Catalytic Domain: The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.Sequence Homology, Amino Acid: The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.Molecular Sequence Data: Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.Sequence Alignment: The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.Cloning, Molecular: The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.Recombinant Proteins: Proteins prepared by recombinant DNA technology.Models, Molecular: Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.Crystallography, X-Ray: The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Protein Conformation: The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).Recombinant Fusion Proteins: Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes.Catalysis: The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.Protein Binding: The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Mutagenesis, Site-Directed: Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.Protein Structure, Secondary: The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to alpha helices, beta strands (which align to form beta sheets) or other types of coils. This is the first folding level of protein conformation.Protein Structure, Tertiary: The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.src Homology Domains: Regions of AMINO ACID SEQUENCE similarity in the SRC-FAMILY TYROSINE KINASES that fold into specific functional tertiary structures. The SH1 domain is a CATALYTIC DOMAIN. SH2 and SH3 domains are protein interaction domains. SH2 usually binds PHOSPHOTYROSINE-containing proteins and SH3 interacts with CYTOSKELETAL PROTEINS.Protein Interaction Domains and Motifs: Protein modules with conserved ligand-binding surfaces which mediate specific interaction functions in SIGNAL TRANSDUCTION PATHWAYS and the specific BINDING SITES of their cognate protein LIGANDS.Escherichia coli: A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.Structure-Activity Relationship: The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups.Kinetics: The rate dynamics in chemical or physical systems.Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.DNA, Complementary: Single-stranded complementary DNA synthesized from an RNA template by the action of RNA-dependent DNA polymerase. cDNA (i.e., complementary DNA, not circular DNA, not C-DNA) is used in a variety of molecular cloning experiments as well as serving as a specific hybridization probe.Amino Acid Motifs: Commonly observed structural components of proteins formed by simple combinations of adjacent secondary structures. A commonly observed structure may be composed of a CONSERVED SEQUENCE which can be represented by a CONSENSUS SEQUENCE.Dimerization: The process by which two molecules of the same chemical composition form a condensation product or polymer.Conserved Sequence: A sequence of amino acids in a polypeptide or of nucleotides in DNA or RNA that is similar across multiple species. A known set of conserved sequences is represented by a CONSENSUS SEQUENCE. AMINO ACID MOTIFS are often composed of conserved sequences.Phosphorylation: The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.Mutation: Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.Sequence Deletion: Deletion of sequences of nucleic acids from the genetic material of an individual.Cellulase: An endocellulase with specificity for the hydrolysis of 1,4-beta-glucosidic linkages in CELLULOSE, lichenin, and cereal beta-glucans.ChitinasePeptide Fragments: Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.DNA Primers: Short sequences (generally about 10 base pairs) of DNA that are complementary to sequences of messenger RNA and allow reverse transcriptases to start copying the adjacent sequences of mRNA. Primers are used extensively in genetic and molecular biology techniques.Transfection: The uptake of naked or purified DNA by CELLS, usually meaning the process as it occurs in eukaryotic cells. It is analogous to bacterial transformation (TRANSFORMATION, BACTERIAL) and both are routinely employed in GENE TRANSFER TECHNIQUES.Mutagenesis: Process of generating a genetic MUTATION. It may occur spontaneously or be induced by MUTAGENS.Bacterial Proteins: Proteins found in any species of bacterium.Enzyme Activation: Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme.Protein Folding: Processes involved in the formation of TERTIARY PROTEIN STRUCTURE.Amino Acid Substitution: The naturally occurring or experimentally induced replacement of one or more AMINO ACIDS in a protein with another. If a functionally equivalent amino acid is substituted, the protein may retain wild-type activity. Substitution may also diminish, enhance, or eliminate protein function. Experimentally induced substitution is often used to study enzyme activities and binding site properties.Hydrolysis: The process of cleaving a chemical compound by the addition of a molecule of water.Cell Line: Established cell cultures that have the potential to propagate indefinitely.Membrane Proteins: Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.DNA: A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine).DNA-Binding Proteins: Proteins which bind to DNA. The family includes proteins which bind to both double- and single-stranded DNA and also includes specific DNA binding proteins in serum which can be used as markers for malignant diseases.Point Mutation: A mutation caused by the substitution of one nucleotide for another. This results in the DNA molecule having a change in a single base pair.PDZ Domains: Protein interaction domains of about 70-90 amino acid residues, named after a common structure found in PSD-95, Discs Large, and Zona Occludens 1 proteins. PDZ domains are involved in the recruitment and interaction of proteins, and aid the formation of protein scaffolds and signaling networks. This is achieved by sequence-specific binding between a PDZ domain in one protein and a PDZ motif in another protein.Protein Structure, Quaternary: The characteristic 3-dimensional shape and arrangement of multimeric proteins (aggregates of more than one polypeptide chain).Signal Transduction: The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway.Saccharomyces cerevisiae: A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement.Cell Membrane: The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.Plasmids: Extrachromosomal, usually CIRCULAR DNA molecules that are self-replicating and transferable from one organism to another. They are found in a variety of bacterial, archaeal, fungal, algal, and plant species. They are used in GENETIC ENGINEERING as CLONING VECTORS.Electrophoresis, Polyacrylamide Gel: Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.Carrier Proteins: Transport proteins that carry specific substances in the blood or across cell membranes.Endo-1,4-beta Xylanases: Enzymes which catalyze the endohydrolysis of 1,4-beta-D-xylosidic linkages in XYLANS.Protein Kinases: A family of enzymes that catalyze the conversion of ATP and a protein to ADP and a phosphoprotein.Transcription Factors: Endogenous substances, usually proteins, which are effective in the initiation, stimulation, or termination of the genetic transcription process.Crystallization: The formation of crystalline substances from solutions or melts. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Enzyme Stability: The extent to which an enzyme retains its structural conformation or its activity when subjected to storage, isolation, and purification or various other physical or chemical manipulations, including proteolytic enzymes and heat.Peptides: Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are linear polypeptides that are normally synthesized on RIBOSOMES.Two-Hybrid System Techniques: Screening techniques first developed in yeast to identify genes encoding interacting proteins. Variations are used to evaluate interplay between proteins and other molecules. Two-hybrid techniques refer to analysis for protein-protein interactions, one-hybrid for DNA-protein interactions, three-hybrid interactions for RNA-protein interactions or ligand-based interactions. Reverse n-hybrid techniques refer to analysis for mutations or other small molecules that dissociate known interactions.Phylogeny: The relationships of groups of organisms as reflected by their genetic makeup.Structural Homology, Protein: The degree of 3-dimensional shape similarity between proteins. It can be an indication of distant AMINO ACID SEQUENCE HOMOLOGY and used for rational DRUG DESIGN.Cellulose: A polysaccharide with glucose units linked as in CELLOBIOSE. It is the chief constituent of plant fibers, cotton being the purest natural form of the substance. As a raw material, it forms the basis for many derivatives used in chromatography, ion exchange materials, explosives manufacturing, and pharmaceutical preparations.Protein Multimerization: The assembly of the QUATERNARY PROTEIN STRUCTURE of multimeric proteins (MULTIPROTEIN COMPLEXES) from their composite PROTEIN SUBUNITS.HeLa Cells: The first continuously cultured human malignant CELL LINE, derived from the cervical carcinoma of Henrietta Lacks. These cells are used for VIRUS CULTIVATION and antitumor drug screening assays.Nuclear Magnetic Resonance, Biomolecular: NMR spectroscopy on small- to medium-size biological macromolecules. This is often used for structural investigation of proteins and nucleic acids, and often involves more than one isotope.Ligands: A molecule that binds to another molecule, used especially to refer to a small molecule that binds specifically to a larger molecule, e.g., an antigen binding to an antibody, a hormone or neurotransmitter binding to a receptor, or a substrate or allosteric effector binding to an enzyme. Ligands are also molecules that donate or accept a pair of electrons to form a coordinate covalent bond with the central metal atom of a coordination complex. (From Dorland, 27th ed)Protein Tyrosine Phosphatases: An enzyme group that specifically dephosphorylates phosphotyrosyl residues in selected proteins. Together with PROTEIN-TYROSINE KINASE, it regulates tyrosine phosphorylation and dephosphorylation in cellular signal transduction and may play a role in cell growth control and carcinogenesis.Glycoside HydrolasesIsoenzymes: Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.Cysteine: A thiol-containing non-essential amino acid that is oxidized to form CYSTINE.Protein-Tyrosine Kinases: Protein kinases that catalyze the PHOSPHORYLATION of TYROSINE residues in proteins with ATP or other nucleotides as phosphate donors.Metalloendopeptidases: ENDOPEPTIDASES which use a metal such as ZINC in the catalytic mechanism.Biocatalysis: The facilitation of biochemical reactions with the aid of naturally occurring catalysts such as ENZYMES.Xylosidases: A group of enzymes that catalyze the hydrolysis of alpha- or beta-xylosidic linkages. EC 3.2.1.8 catalyzes the endo-hydrolysis of 1,4-beta-D-xylosidic linkages; EC 3.2.1.32 catalyzes the endo-hydrolysis of 1,3-beta-D-xylosidic linkages; EC 3.2.1.37 catalyzes the exo-hydrolysis of 1,4-beta-D-linkages from the non-reducing termini of xylans; and EC 3.2.1.72 catalyzes the exo-hydrolysis of 1,3-beta-D-linkages from the non-reducing termini of xylans. Other xylosidases have been identified that catalyze the hydrolysis of alpha-xylosidic bonds.Protein Transport: The process of moving proteins from one cellular compartment (including extracellular) to another by various sorting and transport mechanisms such as gated transport, protein translocation, and vesicular transport.Cercopithecus aethiops: A species of CERCOPITHECUS containing three subspecies: C. tantalus, C. pygerythrus, and C. sabeus. They are found in the forests and savannah of Africa. The African green monkey (C. pygerythrus) is the natural host of SIMIAN IMMUNODEFICIENCY VIRUS and is used in AIDS research.Restriction Mapping: Use of restriction endonucleases to analyze and generate a physical map of genomes, genes, or other segments of DNA.Cricetinae: A subfamily in the family MURIDAE, comprising the hamsters. Four of the more common genera are Cricetus, CRICETULUS; MESOCRICETUS; and PHODOPUS.Nuclear Proteins: Proteins found in the nucleus of a cell. Do not confuse with NUCLEOPROTEINS which are proteins conjugated with nucleic acids, that are not necessarily present in the nucleus.Cellulose 1,4-beta-Cellobiosidase: An exocellulase with specificity for the hydrolysis of 1,4-beta-D-glucosidic linkages in CELLULOSE and cellotetraose. It catalyzes the hydrolysis of terminal non-reducing ends of beta-D-glucosides with release of CELLOBIOSE.Enzyme Precursors: Physiologically inactive substances that can be converted to active enzymes.Fungal Proteins: Proteins found in any species of fungus.Models, Biological: Theoretical representations that simulate the behavior or activity of biological processes or diseases. For disease models in living animals, DISEASE MODELS, ANIMAL is available. Biological models include the use of mathematical equations, computers, and other electronic equipment.Transcription, Genetic: The biosynthesis of RNA carried out on a template of DNA. The biosynthesis of DNA from an RNA template is called REVERSE TRANSCRIPTION.RNA, Messenger: RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.Serine Endopeptidases: Any member of the group of ENDOPEPTIDASES containing at the active site a serine residue involved in catalysis.Sequence Homology, Nucleic Acid: The sequential correspondence of nucleotides in one nucleic acid molecule with those of another nucleic acid molecule. Sequence homology is an indication of the genetic relatedness of different organisms and gene function.Escherichia coli Proteins: Proteins obtained from ESCHERICHIA COLI.Cytoplasm: The part of a cell that contains the CYTOSOL and small structures excluding the CELL NUCLEUS; MITOCHONDRIA; and large VACUOLES. (Glick, Glossary of Biochemistry and Molecular Biology, 1990)Endopeptidases: A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.Polymerase Chain Reaction: In vitro method for producing large amounts of specific DNA or RNA fragments of defined length and sequence from small amounts of short oligonucleotide flanking sequences (primers). The essential steps include thermal denaturation of the double-stranded target molecules, annealing of the primers to their complementary sequences, and extension of the annealed primers by enzymatic synthesis with DNA polymerase. The reaction is efficient, specific, and extremely sensitive. Uses for the reaction include disease diagnosis, detection of difficult-to-isolate pathogens, mutation analysis, genetic testing, DNA sequencing, and analyzing evolutionary relationships.Blotting, Western: Identification of proteins or peptides that have been electrophoretically separated by blot transferring from the electrophoresis gel to strips of nitrocellulose paper, followed by labeling with antibody probes.Sequence Analysis, DNA: A multistage process that includes cloning, physical mapping, subcloning, determination of the DNA SEQUENCE, and information analysis.Glucan 1,4-alpha-Glucosidase: An enzyme that catalyzes the hydrolysis of terminal 1,4-linked alpha-D-glucose residues successively from non-reducing ends of polysaccharide chains with the release of beta-glucose. It is also able to hydrolyze 1,6-alpha-glucosidic bonds when the next bond in sequence is 1,4.Gene Library: A large collection of DNA fragments cloned (CLONING, MOLECULAR) from a given organism, tissue, organ, or cell type. It may contain complete genomic sequences (GENOMIC LIBRARY) or complementary DNA sequences, the latter being formed from messenger RNA and lacking intron sequences.CHO Cells: CELL LINE derived from the ovary of the Chinese hamster, Cricetulus griseus (CRICETULUS). The species is a favorite for cytogenetic studies because of its small chromosome number. The cell line has provided model systems for the study of genetic alterations in cultured mammalian cells.Glutathione Transferase: A transferase that catalyzes the addition of aliphatic, aromatic, or heterocyclic FREE RADICALS as well as EPOXIDES and arene oxides to GLUTATHIONE. Addition takes place at the SULFUR. It also catalyzes the reduction of polyol nitrate by glutathione to polyol and nitrite.Tyrosine: A non-essential amino acid. In animals it is synthesized from PHENYLALANINE. It is also the precursor of EPINEPHRINE; THYROID HORMONES; and melanin.Xylan Endo-1,3-beta-Xylosidase: A xylosidase that catalyses the random hydrolysis of 1,3-beta-D-xylosidic linkages in 1,3-beta-D-xylans.Mutant Proteins: Proteins produced from GENES that have acquired MUTATIONS.Gene Expression: The phenotypic manifestation of a gene or genes by the processes of GENETIC TRANSCRIPTION and GENETIC TRANSLATION.Circular Dichroism: A change from planar to elliptic polarization when an initially plane-polarized light wave traverses an optically active medium. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Precipitin Tests: Serologic tests in which a positive reaction manifested by visible CHEMICAL PRECIPITATION occurs when a soluble ANTIGEN reacts with its precipitins, i.e., ANTIBODIES that can form a precipitate.Evolution, Molecular: The process of cumulative change at the level of DNA; RNA; and PROTEINS, over successive generations.Protein Processing, Post-Translational: Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility.Cattle: Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.Protein-Serine-Threonine Kinases: A group of enzymes that catalyzes the phosphorylation of serine or threonine residues in proteins, with ATP or other nucleotides as phosphate donors.DNA Mutational Analysis: Biochemical identification of mutational changes in a nucleotide sequence.Xylans: Polysaccharides consisting of xylose units.Multigene Family: A set of genes descended by duplication and variation from some ancestral gene. Such genes may be clustered together on the same chromosome or dispersed on different chromosomes. Examples of multigene families include those that encode the hemoglobins, immunoglobulins, histocompatibility antigens, actins, tubulins, keratins, collagens, heat shock proteins, salivary glue proteins, chorion proteins, cuticle proteins, yolk proteins, and phaseolins, as well as histones, ribosomal RNA, and transfer RNA genes. The latter three are examples of reiterated genes, where hundreds of identical genes are present in a tandem array. (King & Stanfield, A Dictionary of Genetics, 4th ed)Magnetic Resonance Spectroscopy: Spectroscopic method of measuring the magnetic moment of elementary particles such as atomic nuclei, protons or electrons. It is employed in clinical applications such as NMR Tomography (MAGNETIC RESONANCE IMAGING).Glycosylation: The chemical or biochemical addition of carbohydrate or glycosyl groups to other chemicals, especially peptides or proteins. Glycosyl transferases are used in this biochemical reaction.COS Cells: CELL LINES derived from the CV-1 cell line by transformation with a replication origin defective mutant of SV40 VIRUS, which codes for wild type large T antigen (ANTIGENS, POLYOMAVIRUS TRANSFORMING). They are used for transfection and cloning. (The CV-1 cell line was derived from the kidney of an adult male African green monkey (CERCOPITHECUS AETHIOPS).)Sequence Analysis: A multistage process that includes the determination of a sequence (protein, carbohydrate, etc.), its fragmentation and analysis, and the interpretation of the resulting sequence information.Dihydrolipoyllysine-Residue Acetyltransferase: An enzyme that catalyzes the acetyltransferase reaction using ACETYL CoA as an acetyl donor and dihydrolipoamide as acceptor to produce COENZYME A (CoA) and S-acetyldihydrolipoamide. It forms the (E2) subunit of the PYRUVATE DEHYDROGENASE COMPLEX.PhosphoproteinsLysine: An essential amino acid. It is often added to animal feed.Zinc Fingers: Motifs in DNA- and RNA-binding proteins whose amino acids are folded into a single structural unit around a zinc atom. In the classic zinc finger, one zinc atom is bound to two cysteines and two histidines. In between the cysteines and histidines are 12 residues which form a DNA binding fingertip. By variations in the composition of the sequences in the fingertip and the number and spacing of tandem repeats of the motif, zinc fingers can form a large number of different sequence specific binding sites.3T3 Cells: Cell lines whose original growing procedure consisted being transferred (T) every 3 days and plated at 300,000 cells per plate (J Cell Biol 17:299-313, 1963). Lines have been developed using several different strains of mice. Tissues are usually fibroblasts derived from mouse embryos but other types and sources have been developed as well. The 3T3 lines are valuable in vitro host systems for oncogenic virus transformation studies, since 3T3 cells possess a high sensitivity to CONTACT INHIBITION.Spodoptera: A genus of owlet moths of the family Noctuidae. These insects are used in molecular biology studies during all stages of their life cycle.Temperature: The property of objects that determines the direction of heat flow when they are placed in direct thermal contact. The temperature is the energy of microscopic motions (vibrational and translational) of the particles of atoms.Serine: A non-essential amino acid occurring in natural form as the L-isomer. It is synthesized from GLYCINE or THREONINE. It is involved in the biosynthesis of PURINES; PYRIMIDINES; and other amino acids.Adaptor Proteins, Signal Transducing: A broad category of carrier proteins that play a role in SIGNAL TRANSDUCTION. They generally contain several modular domains, each of which having its own binding activity, and act by forming complexes with other intracellular-signaling molecules. Signal-transducing adaptor proteins lack enzyme activity, however their activity can be modulated by other signal-transducing enzymesConsensus Sequence: A theoretical representative nucleotide or amino acid sequence in which each nucleotide or amino acid is the one which occurs most frequently at that site in the different sequences which occur in nature. The phrase also refers to an actual sequence which approximates the theoretical consensus. A known CONSERVED SEQUENCE set is represented by a consensus sequence. Commonly observed supersecondary protein structures (AMINO ACID MOTIFS) are often formed by conserved sequences.Intracellular Signaling Peptides and Proteins: Proteins and peptides that are involved in SIGNAL TRANSDUCTION within the cell. Included here are peptides and proteins that regulate the activity of TRANSCRIPTION FACTORS and cellular processes in response to signals from CELL SURFACE RECEPTORS. Intracellular signaling peptide and proteins may be part of an enzymatic signaling cascade or act through binding to and modifying the action of other signaling factors.beta-Mannosidase: An enzyme that catalyzes the hydrolysis of terminal, non-reducing beta-D-mannose residues in beta-D-mannosides. The enzyme plays a role in the lysosomal degradation of the N-glycosylprotein glycans. Defects in the lysosomal form of the enzyme in humans result in a buildup of mannoside intermediate metabolites and the disease BETA-MANNOSIDOSIS.Trypsin: A serine endopeptidase that is formed from TRYPSINOGEN in the pancreas. It is converted into its active form by ENTEROPEPTIDASE in the small intestine. It catalyzes hydrolysis of the carboxyl group of either arginine or lysine. EC 3.4.21.4.Cells, Cultured: Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.Crystallography: The branch of science that deals with the geometric description of crystals and their internal arrangement. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Microscopy, Fluorescence: Microscopy of specimens stained with fluorescent dye (usually fluorescein isothiocyanate) or of naturally fluorescent materials, which emit light when exposed to ultraviolet or blue light. Immunofluorescence microscopy utilizes antibodies that are labeled with fluorescent dye.Protein Subunits: Single chains of amino acids that are the units of multimeric PROTEINS. Multimeric proteins can be composed of identical or non-identical subunits. One or more monomeric subunits may compose a protomer which itself is a subunit structure of a larger assembly.Disulfides: Chemical groups containing the covalent disulfide bonds -S-S-. The sulfur atoms can be bound to inorganic or organic moieties.Macromolecular Substances: Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure.Surface Plasmon Resonance: A biosensing technique in which biomolecules capable of binding to specific analytes or ligands are first immobilized on one side of a metallic film. Light is then focused on the opposite side of the film to excite the surface plasmons, that is, the oscillations of free electrons propagating along the film's surface. The refractive index of light reflecting off this surface is measured. When the immobilized biomolecules are bound by their ligands, an alteration in surface plasmons on the opposite side of the film is created which is directly proportional to the change in bound, or adsorbed, mass. Binding is measured by changes in the refractive index. The technique is used to study biomolecular interactions, such as antigen-antibody binding.Peptide Mapping: Analysis of PEPTIDES that are generated from the digestion or fragmentation of a protein or mixture of PROTEINS, by ELECTROPHORESIS; CHROMATOGRAPHY; or MASS SPECTROMETRY. The resulting peptide fingerprints are analyzed for a variety of purposes including the identification of the proteins in a sample, GENETIC POLYMORPHISMS, patterns of gene expression, and patterns diagnostic for diseases.Molecular Weight: The sum of the weight of all the atoms in a molecule.Immunoblotting: Immunologic method used for detecting or quantifying immunoreactive substances. The substance is identified by first immobilizing it by blotting onto a membrane and then tagging it with labeled antibodies.Repressor Proteins: Proteins which maintain the transcriptional quiescence of specific GENES or OPERONS. Classical repressor proteins are DNA-binding proteins that are normally bound to the OPERATOR REGION of an operon, or the ENHANCER SEQUENCES of a gene until a signal occurs that causes their release.Hydrogen-Ion Concentration: The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)Multienzyme Complexes: Systems of enzymes which function sequentially by catalyzing consecutive reactions linked by common metabolic intermediates. They may involve simply a transfer of water molecules or hydrogen atoms and may be associated with large supramolecular structures such as MITOCHONDRIA or RIBOSOMES.Hydrogen Bonding: A low-energy attractive force between hydrogen and another element. It plays a major role in determining the properties of water, proteins, and other compounds.Protein Isoforms: Different forms of a protein that may be produced from different GENES, or from the same gene by ALTERNATIVE SPLICING.Drosophila Proteins: Proteins that originate from insect species belonging to the genus DROSOPHILA. The proteins from the most intensely studied species of Drosophila, DROSOPHILA MELANOGASTER, are the subject of much interest in the area of MORPHOGENESIS and development.Adenosine Triphosphate: An adenine nucleotide containing three phosphate groups esterified to the sugar moiety. In addition to its crucial roles in metabolism adenosine triphosphate is a neurotransmitter.Alternative Splicing: A process whereby multiple RNA transcripts are generated from a single gene. Alternative splicing involves the splicing together of other possible sets of EXONS during the processing of some, but not all, transcripts of the gene. Thus a particular exon may be connected to any one of several alternative exons to form a mature RNA. The alternative forms of mature MESSENGER RNA produce PROTEIN ISOFORMS in which one part of the isoforms is common while the other parts are different.Threonine: An essential amino acid occurring naturally in the L-form, which is the active form. It is found in eggs, milk, gelatin, and other proteins.HEK293 Cells: A cell line generated from human embryonic kidney cells that were transformed with human adenovirus type 5.Chitin: A linear polysaccharide of beta-1->4 linked units of ACETYLGLUCOSAMINE. It is the second most abundant biopolymer on earth, found especially in INSECTS and FUNGI. When deacetylated it is called CHITOSAN.GTPase-Activating Proteins: Proteins that activate the GTPase of specific GTP-BINDING PROTEINS.Mutation, Missense: A mutation in which a codon is mutated to one directing the incorporation of a different amino acid. This substitution may result in an inactive or unstable product. (From A Dictionary of Genetics, King & Stansfield, 5th ed)Protein Engineering: Procedures by which protein structure and function are changed or created in vitro by altering existing or synthesizing new structural genes that direct the synthesis of proteins with sought-after properties. Such procedures may include the design of MOLECULAR MODELS of proteins using COMPUTER GRAPHICS or other molecular modeling techniques; site-specific mutagenesis (MUTAGENESIS, SITE-SPECIFIC) of existing genes; and DIRECTED MOLECULAR EVOLUTION techniques to create new genes.Proto-Oncogene Proteins: Products of proto-oncogenes. Normally they do not have oncogenic or transforming properties, but are involved in the regulation or differentiation of cell growth. They often have protein kinase activity.Protein Kinase C: An serine-threonine protein kinase that requires the presence of physiological concentrations of CALCIUM and membrane PHOSPHOLIPIDS. The additional presence of DIACYLGLYCEROLS markedly increases its sensitivity to both calcium and phospholipids. The sensitivity of the enzyme can also be increased by PHORBOL ESTERS and it is believed that protein kinase C is the receptor protein of tumor-promoting phorbol esters.Subtilisins: A family of SERINE ENDOPEPTIDASES isolated from Bacillus subtilis. EC 3.4.21.-Gene Deletion: A genetic rearrangement through loss of segments of DNA or RNA, bringing sequences which are normally separated into close proximity. This deletion may be detected using cytogenetic techniques and can also be inferred from the phenotype, indicating a deletion at one specific locus.Molecular Conformation: The characteristic three-dimensional shape of a molecule.Cellulases: A family of glycosidases that hydrolyse crystalline CELLULOSE into soluble sugar molecules. Within this family there are a variety of enzyme subtypes with differing substrate specificities that must work together to bring about complete cellulose hydrolysis. They are found in structures called CELLULOSOMES.Calcium: A basic element found in nearly all organized tissues. It is a member of the alkaline earth family of metals with the atomic symbol Ca, atomic number 20, and atomic weight 40. Calcium is the most abundant mineral in the body and combines with phosphorus to form calcium phosphate in the bones and teeth. It is essential for the normal functioning of nerves and muscles and plays a role in blood coagulation (as factor IV) and in many enzymatic processes.Guanylate Cyclase: An enzyme that catalyzes the conversion of GTP to 3',5'-cyclic GMP and pyrophosphate. It also acts on ITP and dGTP. (From Enzyme Nomenclature, 1992) EC 4.6.1.2.Piromyces: A genus of fungi in the family Neocallimasticaceae, order NEOCALLIMASTICALES, containing uniflagellate zoospores.Nerve Tissue ProteinsGene Expression Regulation, Enzymologic: Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in enzyme synthesis.Enzyme Inhibitors: Compounds or agents that combine with an enzyme in such a manner as to prevent the normal substrate-enzyme combination and the catalytic reaction.Cell Nucleus: Within a eukaryotic cell, a membrane-limited body which contains chromosomes and one or more nucleoli (CELL NUCLEOLUS). The nuclear membrane consists of a double unit-type membrane which is perforated by a number of pores; the outermost membrane is continuous with the ENDOPLASMIC RETICULUM. A cell may contain more than one nucleus. (From Singleton & Sainsbury, Dictionary of Microbiology and Molecular Biology, 2d ed)Complement C1r: A 80-kDa subcomponent of complement C1, existing as a SERINE PROTEASE proenzyme in the intact complement C1 complex. When COMPLEMENT C1Q is bound to antibodies, the changed tertiary structure causes autolytic activation of complement C1r which is cleaved into two chains, A (heavy) and B (light, the serine protease), connected by disulfide bonds. The activated C1r serine protease, in turn, activates COMPLEMENT C1S proenzyme by cleaving the Arg426-Ile427 bond. No fragment is released when either C1r or C1s is cleaved.Allosteric Regulation: The modification of the reactivity of ENZYMES by the binding of effectors to sites (ALLOSTERIC SITES) on the enzymes other than the substrate BINDING SITES.Insects: The class Insecta, in the phylum ARTHROPODA, whose members are characterized by division into three parts: head, thorax, and abdomen. They are the dominant group of animals on earth; several hundred thousand different kinds having been described. Three orders, HEMIPTERA; DIPTERA; and SIPHONAPTERA; are of medical interest in that they cause disease in humans and animals. (From Borror et al., An Introduction to the Study of Insects, 4th ed, p1)Static Electricity: The accumulation of an electric charge on a objectGreen Fluorescent Proteins: Protein analogs and derivatives of the Aequorea victoria green fluorescent protein that emit light (FLUORESCENCE) when excited with ULTRAVIOLET RAYS. They are used in REPORTER GENES in doing GENETIC TECHNIQUES. Numerous mutants have been made to emit other colors or be sensitive to pH.Repetitive Sequences, Amino Acid: A sequential pattern of amino acids occurring more than once in the same protein sequence.Zinc: A metallic element of atomic number 30 and atomic weight 65.38. It is a necessary trace element in the diet, forming an essential part of many enzymes, and playing an important role in protein synthesis and in cell division. Zinc deficiency is associated with ANEMIA, short stature, HYPOGONADISM, impaired WOUND HEALING, and geophagia. It is known by the symbol Zn.Transcriptional Activation: Processes that stimulate the GENETIC TRANSCRIPTION of a gene or set of genes.Calmodulin: A heat-stable, low-molecular-weight activator protein found mainly in the brain and heart. The binding of calcium ions to this protein allows this protein to bind to cyclic nucleotide phosphodiesterases and to adenyl cyclase with subsequent activation. Thereby this protein modulates cyclic AMP and cyclic GMP levels.Open Reading Frames: A sequence of successive nucleotide triplets that are read as CODONS specifying AMINO ACIDS and begin with an INITIATOR CODON and end with a stop codon (CODON, TERMINATOR).Models, Chemical: Theoretical representations that simulate the behavior or activity of chemical processes or phenomena; includes the use of mathematical equations, computers, and other electronic equipment.Thermodynamics: A rigorously mathematical analysis of energy relationships (heat, work, temperature, and equilibrium). It describes systems whose states are determined by thermal parameters, such as temperature, in addition to mechanical and electromagnetic parameters. (From Hawley's Condensed Chemical Dictionary, 12th ed)Nucleic Acid Conformation: The spatial arrangement of the atoms of a nucleic acid or polynucleotide that results in its characteristic 3-dimensional shape.Protozoan Proteins: Proteins found in any species of protozoan.Genetic Complementation Test: A test used to determine whether or not complementation (compensation in the form of dominance) will occur in a cell with a given mutant phenotype when another mutant genome, encoding the same mutant phenotype, is introduced into that cell.Drosophila: A genus of small, two-winged flies containing approximately 900 described species. These organisms are the most extensively studied of all genera from the standpoint of genetics and cytology.Chickens: Common name for the species Gallus gallus, the domestic fowl, in the family Phasianidae, order GALLIFORMES. It is descended from the red jungle fowl of SOUTHEAST ASIA.Phosphoprotein Phosphatases: A group of enzymes removing the SERINE- or THREONINE-bound phosphate groups from a wide range of phosphoproteins, including a number of enzymes which have been phosphorylated under the action of a kinase. (Enzyme Nomenclature, 1992)RNA: A polynucleotide consisting essentially of chains with a repeating backbone of phosphate and ribose units to which nitrogenous bases are attached. RNA is unique among biological macromolecules in that it can encode genetic information, serve as an abundant structural component of cells, and also possesses catalytic activity. (Rieger et al., Glossary of Genetics: Classical and Molecular, 5th ed)Oligodeoxyribonucleotides: A group of deoxyribonucleotides (up to 12) in which the phosphate residues of each deoxyribonucleotide act as bridges in forming diester linkages between the deoxyribose moieties.Hydrophobic and Hydrophilic Interactions: The thermodynamic interaction between a substance and WATER.X-Ray Diffraction: The scattering of x-rays by matter, especially crystals, with accompanying variation in intensity due to interference effects. Analysis of the crystal structure of materials is performed by passing x-rays through them and registering the diffraction image of the rays (CRYSTALLOGRAPHY, X-RAY). (From McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Protein Interaction Mapping: Methods for determining interaction between PROTEINS.ras-GRF1: A guanine nucleotide exchange factor that is expressed primarily in neuronal tissue and may be specific for the Ha-ras homolog of the RAS PROTEINS.Proline: A non-essential amino acid that is synthesized from GLUTAMIC ACID. It is an essential component of COLLAGEN and is important for proper functioning of joints and tendons.Baculoviridae: Family of INSECT VIRUSES containing two subfamilies: Eubaculovirinae (occluded baculoviruses) and Nudibaculovirinae (nonoccluded baculoviruses). The Eubaculovirinae, which contain polyhedron-shaped inclusion bodies, have two genera: NUCLEOPOLYHEDROVIRUS and GRANULOVIRUS. Baculovirus vectors are used for expression of foreign genes in insects.Exons: The parts of a transcript of a split GENE remaining after the INTRONS are removed. They are spliced together to become a MESSENGER RNA or other functional RNA.ras GTPase-Activating Proteins: PROTEINS that specifically activate the GTP-phosphohydrolase activity of RAS PROTEINS.Trans-Activators: Diffusible gene products that act on homologous or heterologous molecules of viral or cellular DNA to regulate the expression of proteins.Sequence Analysis, Protein: A process that includes the determination of AMINO ACID SEQUENCE of a protein (or peptide, oligopeptide or peptide fragment) and the information analysis of the sequence.Phenotype: The outward appearance of the individual. It is the product of interactions between genes, and between the GENOTYPE and the environment.Protein Sorting Signals: Amino acid sequences found in transported proteins that selectively guide the distribution of the proteins to specific cellular compartments.Promoter Regions, Genetic: DNA sequences which are recognized (directly or indirectly) and bound by a DNA-dependent RNA polymerase during the initiation of transcription. Highly conserved sequences within the promoter include the Pribnow box in bacteria and the TATA BOX in eukaryotes.Blotting, Northern: Detection of RNA that has been electrophoretically separated and immobilized by blotting on nitrocellulose or other type of paper or nylon membrane followed by hybridization with labeled NUCLEIC ACID PROBES.

Phenotypic analysis of human glioma cells expressing the MMAC1 tumor suppressor phosphatase. (1/9378)

MMAC1, also known as PTEN or TEP-1, was recently identified as a gene commonly mutated in a variety of human neoplasias. Sequence analysis revealed that MMAC1 harbored sequences similar to those found in several protein phosphatases. Subsequent studies demonstrated that MMAC1 possessed in vitro enzymatic activity similar to that exhibited by dual specificity phosphatases. To characterize the potential cellular functions of MMAC1, we expressed wild-type and several mutant variants of MMAC1 in the human glioma cell line, U373, that lacks endogenous expression. While expression of wild-type MMAC1 in these cells significantly reduced their growth rate and saturation density, expression of enzymatically inactive MMAC1 significantly enhanced growth in soft agar. Our observations indicate that while wild-type MMAC1 exhibits activities compatible with its proposed role as a tumor suppressor, cellular expression of MMAC1 containing mutations in the catalytic domain may yield protein products that enhance transformation characteristics.  (+info)

A processive single-headed motor: kinesin superfamily protein KIF1A. (2/9378)

A single kinesin molecule can move "processively" along a microtubule for more than 1 micrometer before detaching from it. The prevailing explanation for this processive movement is the "walking model," which envisions that each of two motor domains (heads) of the kinesin molecule binds coordinately to the microtubule. This implies that each kinesin molecule must have two heads to "walk" and that a single-headed kinesin could not move processively. Here, a motor-domain construct of KIF1A, a single-headed kinesin superfamily protein, was shown to move processively along the microtubule for more than 1 micrometer. The movement along the microtubules was stochastic and fitted a biased Brownian-movement model.  (+info)

Characterization of the interaction domains of Ure2p, a prion-like protein of yeast. (3/9378)

In the yeast Saccharomyces cerevisiae, the non-Mendelian inherited genetic element [URE3] behaves as a prion. A hypothesis has been put forward which states that [URE3] arises spontaneously from its cellular isoform Ure2p (the product of the URE2 gene), and propagates through interactions of the N-terminal domain of the protein, thus leading to its aggregation and loss of function. In the present study, various N- and C-terminal deletion mutants of Ure2p were constructed and their cross-interactions were tested in vitro and in vivo using affinity binding and a two-hybrid analysis. We show that the self-interaction of the protein is mediated by at least two domains, corresponding to the first third of the protein (the so-called prion-forming domain) and the C-terminal catalytic domain.  (+info)

Purification and identification of a novel subunit of protein serine/threonine phosphatase 4. (4/9378)

The catalytic subunit of protein serine/threonine phosphatase 4 (PP4C) has greater than 65% amino acid identity to the catalytic subunit of protein phosphatase 2A (PP2AC). Despite this high homology, PP4 does not appear to associate with known PP2A regulatory subunits. As a first step toward characterization of PP4 holoenzymes and identification of putative PP4 regulatory subunits, PP4 was purified from bovine testis soluble extracts. PP4 existed in two complexes of approximately 270-300 and 400-450 kDa as determined by gel filtration chromatography. The smaller PP4 complex was purified by sequential phenyl-Sepharose, Source 15Q, DEAE2, and Superdex 200 gel filtration chromatographies. The final product contained two major proteins: the PP4 catalytic subunit plus a protein that migrated as a doublet of 120-125 kDa on SDS-polyacrylamide gel electrophoresis. The associated protein, termed PP4R1, and PP4C also bound to microcystin-Sepharose. Mass spectrometry analysis of the purified complex revealed two major peaks, at 35 (PP4C) and 105 kDa (PP4R1). Amino acid sequence information of several peptides derived from the 105 kDa protein was utilized to isolate a human cDNA clone. Analysis of the predicted amino acid sequence revealed 13 nonidentical repeats similar to repeats found in the A subunit of PP2A (PP2AA). The PP4R1 cDNA clone engineered with an N-terminal Myc tag was expressed in COS M6 cells and PP4C co-immunoprecipitated with Myc-tagged PP4R1. These data indicate that one form of PP4 is similar to the core complex of PP2A in that it consists of a catalytic subunit and a "PP2AA-like" structural subunit.  (+info)

PrKX is a novel catalytic subunit of the cAMP-dependent protein kinase regulated by the regulatory subunit type I. (5/9378)

The human X chromosome-encoded protein kinase X (PrKX) belongs to the family of cAMP-dependent protein kinases. The catalytically active recombinant enzyme expressed in COS cells phosphorylates the heptapeptide Kemptide (LRRASLG) with a specific activity of 1.5 micromol/(min.mg). Using surface plasmon resonance, high affinity interactions were demonstrated with the regulatory subunit type I (RIalpha) of cAMP-dependent protein kinase (KD = 10 nM) and the heat-stable protein kinase inhibitor (KD = 15 nM), but not with the type II regulatory subunit (RIIalpha, KD = 2.3 microM) under physiological conditions. Kemptide and autophosphorylation activities of PrKX are strongly inhibited by the RIalpha subunit and by protein kinase inhibitor in vitro, but only weakly by the RIIalpha subunit. The inhibition by the RIalpha subunit is reversed by addition of nanomolar concentrations of cAMP (Ka = 40 nM), thus demonstrating that PrKX is a novel, type I cAMP-dependent protein kinase that is activated at lower cAMP concentrations than the holoenzyme with the Calpha subunit of cAMP-dependent protein kinase. Microinjection data clearly indicate that the type I R subunit but not type II binds to PrKX in vivo, preventing the translocation of PrKX to the nucleus in the absence of cAMP. The RIIalpha subunit is an excellent substrate for PrKX and is phosphorylated in vitro in a cAMP-independent manner. We discuss how PrKX can modulate the cAMP-mediated signal transduction pathway by preferential binding to the RIalpha subunit and by phosphorylating the RIIalpha subunit in the absence of cAMP.  (+info)

Mechanistic studies on the reductive half-reaction of NADPH-cytochrome P450 oxidoreductase. (6/9378)

Site-directed mutagenesis has been employed to study the mechanism of hydride transfer from NADPH to NADPH-cytochrome P450 oxidoreductase. Specifically, Ser457, Asp675, and Cys630 have been selected because of their proximity to the isoalloxazine ring of FAD. Substitution of Asp675 with asparagine or valine decreased cytochrome c reductase activities 17- and 677-fold, respectively, while the C630A substitution decreased enzymatic activity 49-fold. Earlier studies had shown that the S457A mutation decreased cytochrome c reductase activity 90-fold and also lowered the redox potential of the FAD semiquinone (Shen, A., and Kasper, C. B. (1996) Biochemistry 35, 9451-9459). The S457A/D675N and S457A/D675N/C630A mutants produced roughly multiplicative decreases in cytochrome c reductase activity (774- and 22000-fold, respectively) with corresponding decreases in the rates of flavin reduction. For each mutation, increases were observed in the magnitudes of the primary deuterium isotope effects with NADPD, consistent with decreased rates of hydride transfer from NADPH to FAD and an increase in the relative rate limitation of hydride transfer. Asp675 substitutions lowered the redox potential of the FAD semiquinone. In addition, the C630A substitution shifted the pKa of an ionizable group previously identified as necessary for catalysis (Sem, D. S., and Kasper, C. B. (1993) Biochemistry 32, 11539-11547) from 6.9 to 7.8. These results are consistent with a model in which Ser457, Asp675, and Cys630 stabilize the transition state for hydride transfer. Ser457 and Asp675 interact to stabilize both the transition state and the FAD semiquinone, while Cys630 interacts with the nicotinamide ring and the fully reduced FAD, functioning as a proton donor/acceptor to FAD.  (+info)

Characterization of transgenic mice with targeted disruption of the catalytic domain of the double-stranded RNA-dependent protein kinase, PKR. (7/9378)

The interferon-inducible, double-stranded RNA-dependent protein kinase PKR has been implicated in anti-viral, anti-tumor, and apoptotic responses. Others have attempted to examine the requirement of PKR in these roles by targeted disruption at the amino terminal-encoding region of the Pkr gene. By using a strategy that aims at disruption of the catalytic domain of PKR, we have generated mice that are genetically ablated for functional PKR. Similar to the other mouse model of Pkr disruption, we have observed no consequences of loss of PKR on tumor suppression. Anti-viral response to influenza and vaccinia also appeared to be normal in mice and in cells lacking PKR. Cytokine signaling in the type I interferon pathway is normal but may be compromised in the erythropoietin pathway in erythroid bone marrow precursors. Contrary to the amino-terminal targeted Pkr mouse, tumor necrosis factor alpha-induced apoptosis and the anti-viral apoptosis response to influenza is not impaired in catalytic domain-targeted Pkr-null cells. The observation of intact eukaryotic initiation factor-2alpha phosphorylation in these Pkr-null cells provides proof of rescue by another eukaryotic initiation factor-2alpha kinase(s).  (+info)

His ... Asp catalytic dyad of ribonuclease A: histidine pKa values in the wild-type, D121N, and D121A enzymes. (8/9378)

Bovine pancreatic ribonuclease A (RNase A) has a conserved His ... Asp catalytic dyad in its active site. Structural analyses had indicated that Asp121 forms a hydrogen bond with His119, which serves as an acid during catalysis of RNA cleavage. The enzyme contains three other histidine residues including His12, which is also in the active site. Here, 1H-NMR spectra of wild-type RNase A and the D121N and D121A variants were analyzed thoroughly as a function of pH. The effect of replacing Asp121 on the microscopic pKa values of the histidine residues is modest: none change by more than 0.2 units. There is no evidence for the formation of a low-barrier hydrogen bond between His119 and either an aspartate or an asparagine residue at position 121. In the presence of the reaction product, uridine 3'-phosphate (3'-UMP), protonation of one active-site histidine residue favors protonation of the other. This finding is consistent with the phosphoryl group of 3'-UMP interacting more strongly with the two active-site histidine residues when both are protonated. Comparison of the titration curves of the unliganded enzyme with that obtained in the presence of different concentrations of 3'-UMP shows that a second molecule of 3'-UMP can bind to the enzyme. Together, the data indicate that the aspartate residue in the His ... Asp catalytic dyad of RNase A has a measurable but modest effect on the ionization of the adjacent histidine residue.  (+info)

Mammalian Cdc25 phosphatase is responsible for the dephosphorylation of Cdc2 and other cyclin-dependent kinases at Thr14 and Tyr15, thus activating the kinase and allowing cell cycle progression. The catalytic domain of this dual-specificity phosphatase has recently been mapped to the 180 most C-terminal amino acids. Apart from a CX3R motif, which is present at the active site of all known tyrosine phosphatases, Cdc25 does not share any obvious sequence similarity with any of those enzymes. Until very recently, the Cdc25 family was the only subfamily of tyrosine phosphates for which no three-dimensional structural data were available. Using the generalized profile technique, a sensitive method for sequence database searches, we found an extended and highly significant sequence similarity between the Cdc25 catalytic domain and similarly sized regions in other proteins: the non-catalytic domain of two distinct families of MAP-kinase phosphates, the non-catalytic domain of several ubiquitin protein ...
UCSF researchers have invented a novel method to generate covalent macromolecular inhibitors. This strategy allows a peptide inhibitor to bind to its target protein specifically and irreversibly through proximity-enabled bioreactivity.
The SCOP classification for the Metallo-dependent phosphatases superfamily including the families contained in it. Additional information provided includes InterPro annotation (if available), Functional annotation, and SUPERFAMILY links to genome assignments, alignments, domain combinations, taxonomic visualisation and hidden Markov model information.
ウサギ・ポリクローナル抗体 ab96186 交差種: Ms,Hu 適用: WB,ICC/IF…cAMP Protein Kinase Catalytic subunit抗体一覧…画像、プロトコール、文献などWeb上の情報が満載のアブカムの Antibody…
Enzymes are nanomachines that are exceptionally efficient at catalyzing a chemical reaction. They play a role in all cellular mechanisms. Like all proteins, they are made up of amino acid chains that are folded and assembled in a very precise 3D structure. Some enzymes, like ribonuclease A, are so efficient that they catalyze the transformation of chemical molecules thousands of times per second.. In this study, Donald Gagné, a researcher in Professor Doucets lab holding a PhD in biology from INRS, analyzed the impact of removing a methyl group located near a loop distant from the reaction site of ribonuclease A-a very slight change that presumably would have no effect. The mutation does not perturb the 3D structure of the enzyme. However, it did result in a four-fold reduction in the affinity of ribonuclease A for nucleotides (molecules to which it must bind to carry out its function). How is this possible?. Using crystallography techniques and nuclear magnetic resonance to examine the enzyme ...
BioAssay record AID 1078796 submitted by ChEMBL: Inhibition of human FER catalytic domain expressed in baculovirus assessed as substrate phosphorylation using fluorescence-labelled peptides as substrate at 9 uM after 90 mins by microfluidic peptide phosphorylation assay.
BioAssay record AID 1078341 submitted by ChEMBL: Inhibition of human IRAK4 catalytic domain expressed in baculovirus assessed as substrate phosphorylation using fluorescence-labelled peptides as substrate at 1000 uM after 90 mins by microfluidic peptide phosphorylation assay.
1GNR: X-ray crystal structure analysis of the catalytic domain of the oncogene product p21H-ras complexed with caged GTP and mant dGppNHp.
Read "Three Cdk1 sites in the kinesin-5 Cin8 catalytic domain coordinate motor localization and activity during anaphase, Cellular and Molecular Life Sciences" on DeepDyve, the largest online rental service for scholarly research with thousands of academic publications available at your fingertips.
, MDC Recombinant Protein (Active), GTX48056-PRO, Applications: ELISA, WB, Functional Assay; ELISA, Western Blot (WB), Functional Assay; CrossReactivity:
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
DI-fusion, le Dépôt institutionnel numérique de lULB, est loutil de référencementde la production scientifique de lULB.Linterface de recherche DI-fusion permet de consulter les publications des chercheurs de lULB et les thèses qui y ont été défendues.
appendicitis - Meaning in Thai, what is meaning of common in Thai dictionary, audio pronunciation, synonyms and definitions of common in Thai and English.
Diflavin reductases are essential proteins capable of splitting the two-electron flux from reduced pyridine nucleotides to a variety of one electron acceptors. The primary sequence of diflavin reductases shows a conserved domain organization harboring two catalytic domains bound to the FAD and FMN flavins sandwiched by one or several non-catalytic domains. The catalytic domains are analogous to existing globular proteins: the FMN domain is analogous to flavodoxins while the FAD domain resembles ferredoxin reductases. The first structural determination of one member of the diflavin reductases family raised some questions about the architecture of the enzyme during catalysis: both FMN and FAD were in perfect position for interflavin transfers but the steric hindrance of the FAD domain rapidly prompted more complex hypotheses on the possible mechanisms for the electron transfer from FMN to external acceptors. Hypotheses of domain reorganization during catalysis in the context of the different members of
Electrostatic interactions between ligands and their receptors are important factors for molecular recognition. Assessing the ligand-receptor electrostatic complementarity provide valuable information for molecular design. In this hands-on workshop we will focus on using Flare™, Cressets structure-based design application to design ligands that are electrostatically complementary to the protein active site. You will learn how to visualize ligand-protein interactions; design new molecules in the context of the active site; easily dock new molecule designs to a protein active site; and assess the electrostatic complementarity between ligands and protein.
Scientists at the Center for Molecular Electrocatalysis conducted a detailed comparison of catalytic performance. They compared catalysts with different ring sizes and different numbers of proton relays. They found that the catalyst 7P2N with a smaller ring and fewer proton relays was faster or had a higher turnover efficiency. CME is an Energy Frontier Research Center funded by DOE Basic Energy Sciences and led by Pacific Northwest National Laboratory
1CBO: Crystal structure determination of cholesterol oxidase from Streptomyces and structural characterization of key active site mutants.
Of course much of human biology - growth and development, and cancer metastasis are the big ones - rely on these sensing and adhesion mechanisms, but Geiger and Spatz bring up some others: How certain cells sense blood flow, for instance, might affect the sticky buildup of plaques on artery walls. And they suggest that even before primitive cells began sticking together to form multicellular organisms, they probably formed some version of these complexes to adhere to other things - food sources, for instance.. The second article describes the postdoctoral research and future plans of Dr. Sarel Fleishman, who recently joined the Institute. Fleishman was in the protein design lab of Prof. David Baker at the University of Washington, Seattle, where he designed a protein that is able to block a wide range of flu viruses.. "Designed" is the operative word here: Fleishman and his lab mates showed that one can predict what is needed to selectively bind to a virus proteins active site, create a ...
Sigma-Aldrich offers abstracts and full-text articles by [Rasha H Alghamdi, Paul OReilly, Chunyu Lu, James Gomes, Thomas A Lagace, Ajoy Basak].
Mutations are changes in the base sequence of DNA, these mutations can produce new alleles of genes, if this changes a different protein or a non-functioning protein (change in the structure leading to a wrong active site) can be produced. ...
The Enzyme Collection contains over 550 mAbs that recognize catalytic domains or associated regulatory subunits in enyme complexes
A molecule that doesnt have a similar shape to the substrate, but binds elsewhere than the active site. This changes the shape of the enzyme and the active site, meaning that the substrate can no longer fit. Therefore, no reaction occurs. ...
Within biological systems iron is a transition metal that allows access to the benefits of molecular oxygen as an oxidant. However, with these benefits come grave consequences if the reactions are not strictly controlled. The most prominent strategy of control and specialization is the protein environment that surrounds iron. Within iron containing proteins, specifically heme proteins, there are four basic levels of structure that impact the irons function: cofactor structure, protein-supplied ligands, non-ligand active site environment, and protein features that are distant from the active site. This last level remains poorly understood due to a lack of good models to pursue such studies. Catalase-peroxidases are unique heme proteins because they catalyze peroxide decomposition by two separate mechanisms, catalase and peroxidase, using the same active site. However, were it not for three structural features distant from the active site, catalase-peroxidases would be practically superimposable ...
Eukaryotic protein kinases [1,2,3,4,5] are enzymes that belong to a very extensive family of proteins which share a conserved catalytic core common to both serine/threonine and tyrosine protein kinases. There are a number of conserved regions in the catalytic domain of protein kinases. We have selected two of these regions to build signature patterns. The first region, which is located in the N-terminal extremity of the catalytic domain, is a glycine-rich stretch of residues in the vicinity of a lysine residue, which has been shown to be involved in ATP binding. The second region, which is located in the central part of the catalytic domain, contains a conserved aspartic acid residue which is important for the catalytic activity of the enzyme [6]; we have derived two signature patterns for that region: one specific for serine/ threonine kinases and the other for tyrosine kinases. We also developed a profile which is based on the alignment in [1] and covers the entire catalytic domain. Note: If a ...
Eukaryotic protein kinases [1,2,3,4,5] are enzymes that belong to a very extensive family of proteins which share a conserved catalytic core common to both serine/threonine and tyrosine protein kinases. There are a number of conserved regions in the catalytic domain of protein kinases. We have selected two of these regions to build signature patterns. The first region, which is located in the N-terminal extremity of the catalytic domain, is a glycine-rich stretch of residues in the vicinity of a lysine residue, which has been shown to be involved in ATP binding. The second region, which is located in the central part of the catalytic domain, contains a conserved aspartic acid residue which is important for the catalytic activity of the enzyme [6]; we have derived two signature patterns for that region: one specific for serine/ threonine kinases and the other for tyrosine kinases. We also developed a profile which is based on the alignment in [1] and covers the entire catalytic domain. Note: If a ...
Mono- and Stereopictres of 5.0 Angstrom coordination sphere of Zinc atom in PDB 3frg: Catalytic Domain of Human Phosphodiesterase 4B2B in Complex With A Quinoline Inhibitor
New insights into the behaviour of molecules could have major implications for the design of drugs that block protein interactions. A team of researchers led by Dr Peter Crowley at the National University of Ireland Galway has revealed in intricate detail how a drug-like molecule can explore the surface of a protein.. The pioneering work was published by Nature Chemistry online (Sunday, 29 April) and will appear in the June issue of the journal. It was found that molecules scout around the protein surface, moving from one location to another constantly examining their surroundings.. For the past thirty years, drug design has been dominated by the search for small molecules that fit perfectly into a proteins active site and modify its activity. Recently, the focus of attention has shifted to molecules that recognise and bind to the protein surface. Such molecules can camouflage the protein and prevent it binding to other proteins. Knowledge of these interactions is essential to the development ...
These enzymes are very specific, Dordick said, targeting one or only a few bacteria. In this paper, the researchers set out to see if they could improve the combinations nature has created.. "The idea was: Could we use a Lego-like approach here? Could we take a binding domain from one enzyme and can we mix it with a binding domain or catalytic domain of another one?" Dordick said.. More specifically, the team took the protein streptavidin, which acts as an effective template to which the researchers could attach a binding domain from one organism and a catalytic domain from another. The modularity approach allows them to make new combinations quickly in order to determine which work best.. They found that in targeting Staphylococcus aureus - commonly known as staph - their combinations were very effective, at times even better than what occurs in nature.. "We genetically expressed the binding domains or the catalytic domains from several different organisms," Dordick said. "We identified some ...
, GDF8 / Myostatin Recombinant Protein (Active), GTX48445-PRO, Applications: ELISA, WB, Functional Assay; ELISA, Western Blot (WB), Functional Assay; CrossReactivity:
Purpose Metabolism, and especially glucose uptake, is normally an integral quantitative cell characteristic thats associated with cancer tumor initiation and development closely. advantages within the various other available blood sugar tracers, such as for example 2-DG or the radiolabel isotope FDG, including INCB8761 its low comparative cost, convenience of high temporal and spatial quality (on the single-cell level), insufficient ionizing radiation, as well as the nondestructive nature enabling immediate monitoring of blood sugar transport in live cells. Furthermore, we developed another independent method of directly measure the distribution of blood sugar uptake on the single-cell level that utilizes the energy of high-content computerized microscopy (HCAM), cell-cytometric picture evaluation (via in DMSO. Likewise, split plates had been treated and ready with Erlotinib at the same concentrations. Cells had been incubated with medications for another INCB8761 24 h Cish3 under regular ...
AbeBooks.com: Enzymic Catalysis (Modern Perspectives in Biology): Spine creases, wear to binding and pages from reading. May contain limited notes, underlining or highlighting that does affect the text. Possible ex library copy, thatâ ll have the markings and stickers associated from the library. Accessories such as CD, codes, toys, may not be included.
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
Business Gurus:. "…In this article, Jim Collins introduces the catalytic mechanism, a simple yet powerful managerial tool that helps translate lofty aspirations into concrete reality. Whats the difference between catalytic mechanisms and most traditional managerial controls? Catalytic mechanisms share five characteristics. First, they produce desired results in unpredictable ways. Second, they distribute power for the benefit of the overall system, often to the discomfort of those who traditionally hold power. Third, catalytic mechanisms have teeth. Fourth, they eject viruses--those people who dont share the companys core values. Finally, they produce an ongoing effect.". [Editorial Review, Book Description of Turning Goals into Results: The Power of Catalytic Mechanisms by Jim Collins posted at www.amazon.com ]. "Now that we are really beginning to understand what makes organizations great in the business world, we might actually provide some DNA to the whole social system." ...
The Enzyme Collection contains over 550 mAbs that recognize catalytic domains or associated regulatory subunits in enyme complexes
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of HIV-1 protease is inhibited by Crixivan when the molecule interacts with the specific sites that a Gag protein peptide would normally interact with. The active site contains Asp25, which is involved in peptide cleavage, Thr26, which is involved in stabilizing the active site conformation, and Gly27, which is involved in the binding of a protein in a position that gives Asp25 access to its cleavage site.[3] Arg8 also plays a role in holding a substrate in place in the enzyme active site. When the Crixivan molecule enters the protease active site it imitates the transition state of Gag protein peptides during the cleavage reaction. The virus peptide bonds [-NH-CO-] can be cleaved via aspartic catalysis[1]. Crixivan contains a hydroxyethylene [-CH2-CH(OH)-] site instead that cannot be cleaved by Asp25.[4] The molecule becomes stuck inside the active site because of the hydrogen bonds between Arg8 and Crixivans pyridine ring and the interactions between Gly27 and Crixivans aromatic rings.[5] ...
Mono- and Stereopictres of 5.0 Angstrom coordination sphere of Zinc atom in PDB 1tbf: Catalytic Domain of Human Phosphodiesterase 5A in Complex With Sildenafil
For additional Rizzo Lab tutorials see [[DOCK Tutorials]]. This tutorial is based on the [[2010 DOCK tutorial with Streptavidin]] with minor modifications. ==About DOCK== DOCK was developed by Irwin D. "Tack" Kuntz, Jr., PhD and colleagues at UCSF. Please see the webpage at [http://dock.compbio.ucsf.edu/ UCSF DOCK]. DOCK is a molecular docking program used in drug discovery. This program, given a protein active site and a small molecule, tries to predict the correct binding mode of the small molecule in the active site, and the associated binding energy. Small molecules with highly favorable binding energies could be new drug leads. This makes DOCK a valuable drug discovery tool. DOCK is typically used to screen massive libraries of millions of compounds against a protein to isolate potential drug leads. These leads are then further studied, and could eventually result in a new, marketable drug. DOCK is works well as a screening procedure for generating leads, but not nearly as well for ...
For additional Rizzo Lab tutorials see [[DOCK Tutorials]]. This tutorial is based on the [[2010 DOCK tutorial with Streptavidin]] with minor modifications. ==About DOCK== DOCK was developed by Irwin D. "Tack" Kuntz, Jr., PhD and colleagues at UCSF. Please see the webpage at [http://dock.compbio.ucsf.edu/ UCSF DOCK]. DOCK is a molecular docking program used in drug discovery. This program, given a protein active site and a small molecule, tries to predict the correct binding mode of the small molecule in the active site, and the associated binding energy. Small molecules with highly favorable binding energies could be new drug leads. This makes DOCK a valuable drug discovery tool. DOCK is typically used to screen massive libraries of millions of compounds against a protein to isolate potential drug leads. These leads are then further studied, and could eventually result in a new, marketable drug. DOCK is works well as a screening procedure for generating leads, but not nearly as well for ...
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Purpose Metabolism, and especially glucose uptake, is normally an integral quantitative cell characteristic thats associated with cancer tumor initiation and development closely. advantages within the various other available blood sugar tracers, such as for example 2-DG or the radiolabel isotope FDG, including INCB8761 its low comparative cost, convenience of high temporal and spatial quality (on the single-cell level), insufficient ionizing radiation, as well as the nondestructive nature enabling immediate monitoring of blood sugar transport in live cells. Furthermore, we developed another independent method of directly measure the distribution of blood sugar uptake on the single-cell level that utilizes the energy of high-content computerized microscopy (HCAM), cell-cytometric picture evaluation (via in DMSO. Likewise, split plates had been treated and ready with Erlotinib at the same concentrations. Cells had been incubated with medications for another INCB8761 24 h Cish3 under regular ...
Exceptions to a long-held rule against chemically bonding to biological targets are powering new cancer medicines, finds Andy Extance
Modules of approx. 70 residues. The chitin-binding function has been demonstrated in several cases. These modules are found attached to a number of chitinase catalytic domains, but also in non-catalytic proteins either in isolation or as multiple repeats; chitin binding (EC IIa.chitin ...
... focuses on the rapid publication of original invited papers devoted to currently important topics in catalysis and related subjects....
鳳嬌紙樣卡提供A5尺寸紙張及紙張所有詳細資訊卡,可做簡單試用或個人收藏。. 裸棉紙在製程中未經漂白,透過人工一一剔除雜質,並非全然淨白的紙面保有了原始真實的纖維質地,散發自然光澤。. 產地製造| 台灣 / 手工 ...
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Domain combinations containing the Carbohydrate phosphatase superfamily in Pasteurella multocida subsp. multocida str. Pm70. Domain architectures illustrate each occurrence of the Carbohydrate phosphatase superfamily.
Abstract: Thioesterases catalyze the cleavage of thioester bonds within many activated fatty acids and acyl-CoA substrates. They are expressed ubiquitously in both prokaryotes and eukaryotes and are subdivided into 25 thioesterase families according to their catalytic active site, protein oligomerization, and substrate specificity. While many of these enzyme families are well characterized in terms of function and substrate specificity, regulation across most thioesterase families is poorly understood. Here, we characterized a TE6 thioesterase from the bacterium Neisseria meningitidis. Structural analysis with X-ray crystallographic diffraction data to 2.0 Å revealed that each protein subunit harbors a hot dog fold and that the TE6 enzyme forms a hexamer with D3 symmetry. An assessment of thioesterase activity against a range of acyl-CoA substrates revealed greatest activity against acetyl-CoA, and structure-guided mutagenesis of putative active site residues identified Asn-24 and Asp-39 as ...
In recent years, members of the protein kinase family have been discovered at an accelerated pace. Most were first described, not through the traditional biochemical approach of protein purification and enzyme assay, but as putative protein kinase amino acid sequences deduced from the nucleotide sequences of molecularly cloned genes or complementary DNAs. Phylogenetic mapping of the conserved protein kinase catalytic domains can serve as a useful first step in the functional characterization of these newly identified family members. ...
FeFe]-Hydrogenases (H2ases) are metalloenzymes that can catalyze the reversible reduction of protons to molecular hydrogen as part of the metabolism of certain cyanobacteria and green algae. Due to the low availability of the enzyme, synthetic complexes that mimic the natural active site in structure, function and activity are highly sought after. In this thesis, a number of [FeFe]-H2ases active site model complexes were synthesized to answer open questions of the active site and to develop unprecedented bio-inspired proton reduction catalysts.. The first part describes the synthesis and the protonation properties of a [Fe2(μ-adt)(CO)4(PMe3)2] (adt = azadithiolate) complex which contains two basic sites that are similar to those found in the enzyme active site. Unusual kinetic factors give rise to four discrete protonation states. The twofold protonated state is the first model complex that simultaneously carries a proton at the azadithiolate nitrogen and a bridging hydride at the Fe-Fe ...
The catalytic subunit of type 1 protein phosphatase (PP1C) interacts with a large number of polypeptides in eukaryotic cells from yeast to man and these regulatory subunits can both modulate the activ
glutamate-cysteine ligase complex, enzyme regulator activity, glutamate-cysteine ligase activity, glutamate-cysteine ligase catalytic subunit binding, protein heterodimerization activity, aging, apoptotic mitochondrial changes, cellular response to fibroblast growth factor stimulus, cellular response to follicle-stimulating hormone stimulus, cellular response to glucose stimulus
Mono- and Stereopictres of 5.0 Angstrom coordination sphere of Bromine atom in PDB 1zpz: Factor XI Catalytic Domain Complexed With N-((R)-1-(4- Bromophenyl)Ethyl)Urea-Asn-Val-Arg-Alpha-Ketothiazole
Protein Phosphatase 1: A eukayrotic protein serine-threonine phosphatase subtype that dephosphorylates a wide variety of cellular proteins. The enzyme is comprised of a catalytic subunit and regulatory subunit. Several isoforms of the protein phosphatase catalytic subunit exist due to the presence of multiple genes and the alternative splicing of their mRNAs. A large number of proteins have been shown to act as regulatory subunits for this enzyme. Many of the regulatory subunits have additional cellular functions.
The catalytic nucleophile is an aspartate, while the catalytic acid-base is a histidine. The later is unusual in GHs, and a divergence from GH29, but is likely necessary to avoid electronic repulsion with the substrate sulfate groups. These two residues have been identified by structural superimposition with GH29 enzymes, and are conserved within the few members of the GH107 family. The catalytic His has been further confirmed by the lack of activity of the H294Q mutant of Mariniflexile fucanivorans [2]. The catalytic aspartate was also proposed to be one of the catalytic residue on sequence analysis alone, in a simultaneously released paper [3]. ...
Substrate cleavage by metalloproteinases involves nucleophilic attack on the scissile peptide bond by a water molecule that is polarized by a catalytic metal, usually a zinc ion, and a general base, usually the carboxyl group of a glutamic acid side chain
This is another method in which an enzyme active site can bring in certain elements of substrates, while repelling other people to create the suitable fit. Thus the accession of a sample is dependent upon the range of samples we have. All content is strictly informational https://en.wikipedia.org/wiki/George_Dantzig and should not be regarded as medical advice.. Exogenous antigens are the most frequent kinds of antigens, and includes pollen or foods that might cause allergies, and the molecular elements of bacteria and other pathogens that could lead to an infection. Some lymphocytes work alone, while some can coordinate with different cells. These cells are a valuable part of the immune system since they have the ability to recognize virally infected cells, along with some kinds of tumor cells, and kill them before they cause an outstanding quantity of harm.. Pneumonia can lead to a drop in lymphocytes. Subsequent infections will be a lot less dangerous, because the active immunity will signify ...
reference: Crystal structure of the catalytic domain of human plasmin complexed with streptokinase., Wang X, Lin X, Loy JA, Tang J, Zhang XC, Science 1998 Sep 11;281(5383):1662-5. PMID: 9733510 ...
Published in J. Phys. Chem. B, 2010. Recommended citation: Jing Zhao, Chang Lu, Stefan Franzen*, J. Phys. Chem. B, 2015,119 (40), pp 12828-12837. http://pubs.acs.org/doi/abs/10.1021/acs.jpcb.5b07126 ...
ramiuk1. 30 tablets isnt alot tbh(unless its 1 a day and then they be huge!!) … 30 tablets isnt alot tbh(unless its 1 a day and then they be huge!!) ,also good quality stuff is always around a decent price anyway so i would go with branded stuff over this. ...
Zagraniczne książki pl - medycyna - bogaty zbiór książek w oryginalnych wydaniach, wydawnictwa zagraniczne, ksiązki zagraniczne.
Księgarnia wysyłkowa online - oferujemy audiobooki, ebooki, książki i czasopisma naukowe, ekonomiczne, prawnicze i wiele innych. Sprawdź - księgarnia internetowa Warszawa. Zapraszamy.
bph:Bphy_5237 K05343 maltose alpha-D-glucosyltransferase / alpha-amylase [EC:5.4.99.16 3.2.1.1] , (GenBank) alpha amylase catalytic region (A) MLNDLWYKNAIIYCLSVGTFMDANGDGIGDFAGLMRRLDYLQGLGITAIWLMPIQPSPGR DNGYDVSDYYNVDPKYGTLGDFAEFTHACAERGLRVIIDLVVNHTSDQHPWFKEARSDPD SKYRDWYVWADKKPPDATHGVAFPGVQKSTWSFDKRARRWYFHRFYDFQPDLNTSNPHVQ AELLKIMGFWIQLGVSGFRMDAVPFVIATKGPKVREPVEQYEMLRSFREFLQWREGDAII LAEANVLPDTDLEYFGEEGERLPMMFNFQLNQNTFYTLATGDTKPLKHALLATKPRPPSA QWGVFLRNHDELDLGRLTPEQRAAVFAAFGPEPGMQLYQRGIRRRLAPMLAGDRRHLELA YSLMLSLPGTPVFRYGDEIGMGDDLRRPERACARTPMQWSTEPQGGFTKHTRPPVSVISG GPYGFERVNVATQRRDPNSLLNWMERMIRMRKEVPEISWGDFEVLRTSRSDVLALCYHWR NNSVLFLHNFAAKACTVKFRSGCNEPVGCPLINLLSDDHSQPGDDGRHAVVLEPYGYRWY RVGGLDYLLTRSEI ...
... publishes original papers on all aspects of catalysis of basic and practical interest to chemical scientists in both...
Catalysis is a process that accelerates a chemical reaction and makes it possible to turn a great variety of resources into important and necessary products
hirutonin-2: an analog of (D)Phe-Pro-Arg-Gly-hirudin(49-65); binds to thrombin active site and forms a complex; structure in first source
Little is known about the active site of guanylate cyclase, although it is assigned to a 239-amino acid region (catalytic domain).4 Since the catalytic domain of guanylate cyclase (GC-c) can be functionally expressed as a soluble protein in E coli, it, rather than the whole enzyme, may be an ideal system for studying the active site of guanylate cyclase. Using guanylate cyclase assay, we screened several PCR-cloned gene products of GC-c and identified a mutant that lacks enzyme activity. Results of cDNA sequencing revealed that Leu 817 is converted into an Arg residue in the mutant. Sequence comparison reveals that Leu 817 is conserved in the corresponding position of most known guanylate cyclases and adenylate cyclases. These results suggest that Leu 817 of guanylate cyclase may play an important functional or structural role.. GC-A has been reported to form oliogomers (dimer, tetramer, and possibly higher order oligomers) in the absence of ANF, and the extracellular receptor sequence has been ...
Altering the characteristics of an active-site loop in an (S)-selective omega-transaminase from Arthrobacter citreus (variant CNB05-01) influences the enantioselectivity. This active-site loop belongs to the second subunit of the dimeric enzyme structure that participates in the coordination of pyridoxal-5-phosphate (PLP) in the so called "phosphate group binding cup". Three amino acid residues (E326, V328, and Y331) in this loop are selected by homology modeling for site-directed mutagenesis aiming to increase the enzyme enantioselectivity for 4-fluorophenylacetone. By combining these mutations, five enzyme variants are created. The performance of these variants is explored using a model system consisting of isopropylamine and 4-fluorophenylacetone or 4-nitroacetophenone in asymmetric synthesis using a whole-cell system approach. Three of the five variants show increased enantioselectivity for 4-fluorophenylacetone compared to CNB05-01. Variant CNB05-01/Y331C increases the enantioselectivity ...
Glutamate-cysteine ligase, also known as gamma-glutamylcysteine synthetase is the first rate-limiting enzyme of glutathione synthesis. The enzyme consists of two subunits, a heavy catalytic subunit and a light regulatory subunit. This locus encodes the catalytic subunit, while the regulatory subunit is derived from a different gene located on chromosome 1p22-p21. Mutations at this locus have been associated with hemolytic anemia due to deficiency of gamma-glutamylcysteine synthetase and susceptibility to myocardial infarction.[provided by RefSeq, Oct 2010 ...
Mediates cAMP-dependent signaling triggered by receptor binding to GPCRs. PKA activation regulates diverse cellular processes such as cell proliferation, the cell cycle, differentiation and regulation of microtubule dynamics, chromatin condensation and decondensation, nuclear envelope disassembly and reassembly, as well as regulation of intracellular transport mechanisms and ion flux. Regulates the abundance of compartmentalized pools of its regulatory subunits through phosphorylation of PJA2 which binds and ubiquitinates these subunits, leading to their subsequent proteolysis ...
The Chang Lab, 2015. Transition Metal Signaling. Our laboratory has advanced a new paradigm of transition metal signaling, where essential elements like copper and iron can serve as dynamic regulators of biological function. This concept broadens the traditional view of metals in biology that narrowly defines these and other redox-active elements as static metabolic cofactors that must tightly-bound within buried protein active sites to protect against oxidative stress, and with only redox-innocent metals (e.g., sodium, potassium, calcium, zinc) having the capacity to serve as mobile signals. We are developing activity-based sensing (ABS) probes and related chemical tools for imaging dynamic transition metal pools by fluorescence, bioluminescence and MRI, as well as for proteomic identification and characterization of new metalloprotein targets. These technologies are being applied in cell, tissue, zebrafish, and mouse models to study the contributions of transition metal signaling to fat ...
Enzyme catalysis can be regarded as a catalytic reaction between homogeneous and heterogeneous reactions. It can be seen as the reaction between the enzyme and the reaction for formation of intermediate compounds, and it can also be seen as the reaction after the surface of the enzyme adsorbs the reactant.. What are enzymes?. It is an organic colloidal substance composed of protein. It plays a catalytic role for biochemical reactions.. Fermentation also is finished by its role of protease enzyme.. Enzyme catalysis. Accelerating or slowing down a chemical reaction by enzymes is called enzyme catalysis. Hundreds of different reactions performing simultaneously in a living cell are accomplished by a considerable number of enzymes. In many cases, small structural changes in the substrate molecule will make the compound loss the ability to act as a substrate.. Features. Enzyme catalysis shows a characteristic which is not seen in non-enzymatic reaction. It can be saturated with substrate. When the ...
Studies using PKC regulatory/catalytic domain chimeras have underscored the complexity of PKC functions in relation to its structural domains. In previous reports, we and others showed that certain features of isozyme-specific PKC functions could be attributed to the catalytic domain only. These include the PKC-δ-mediated PMA-induced macrophage differentiation of 32D cells (14), the tumorigenicity of PKC-ε-overexpressing NIH 3T3 cells (15), the PKC-βII-mediated growth promotion in K-562 cells (26), and the protection of PKC-δ from down-regulation induced by bryostatin 1 in NIH 3T3 cells (17). However, in some cases, both the regulatory and the catalytic domains contribute to the isoform-specific effects (15, 18, 27). Further mapping of the structural domains beyond the catalytic and regulatory regions is essential to clearly determine the function of each structural domain and to understand how individual domains interact with each other to regulate PKC function.. Previous studies on the ...
Shieh HS, Mathis KJ, Williams JM, Hills RL, Wiese JF, Benson TE, Kiefer JR, Marino MH, Carroll JN, Leone JW, Malfait AM, Arner EC, Tortorella MD, Tomasselli A. High resolution crystal structure of the catalytic domain of ADAMTS-5 (aggrecanase-2). J Biol Chem. 2008 Jan 18; 283(3):1501-7 ...
Recombinant full-length human STK3 was expressed by baculovirus in Sf9 insect cells using a N-terminal GST tag. STK3, also known as MST2, encodes a protein of 491-amino acid which contains an N-terminal catalytic domain characteristic of STKs.
Get an in-depth review and ask questions about Specific versus General Acid Catalysis. See what people are saying about Specific versus General Acid Catalysis.
Finds sub-sequences or patterns in the sequence and highlights the matching regions. The tool works with standard single letter nucleotide or protein codes including ambiguities and can match Prosite patterns in protein sequences. More... ...
The track record of man-made enzyme mimetics is not impressive. I previously commented that, time and again, we get beaten by natures enzymes in terms of catalytic efficiency. If we consider hydrolases, it is all about the spatiotemporal relationship between their catalytic amino acid residues and the peptide bond that is being cleaved. Things happen…
What we have here is the re-identification of a known thiol-reactive molecule without any acknowledgement or apparent awareness that the molecule is reactive. I have no problem with covalent inhibitors, but I do have a problem with a generically reactive molecule being touted "for a future lead development", as the researchers state in the abstract. It took me just minutes to track down the references above, and the fact that neither the researchers nor the reviewers did so is inexcusable ...
But one would still expect a geometric factor to come into play - substrate needs to reach the enzyme from the right side in order to bind. Working at exactly diffusion limit implies that this geometric factor does not exist - the enzyme conveys substrate toward/into active site no matter how they bumped into each other. Ive seen references to the enzymes exceeding diffusion limits but, personally, I do not understand how it is possible. The thats because the active site is surrounded by charged residues that attract oppositely charged substrate molecules! does not cut it because it implies that the substrate is moving directionally (and faster than diffusion) under the influence of coulombic force, which is, I think, too weak for that.. Delete ...
Other articles where Inhibitor is discussed: catalysis: …a foreign substance, called an inhibitor, decreases the rate of a chemical reaction. This phenomenon, properly termed inhibition or retardation, is sometimes called negative catalysis. Concentrations of the inhibitor may in some cases be much lower than those of the reactants. Inhibition may result from (1) a decrease in the…
Wydawnictwo medyczne Cornetis publikuje czasopisma dedykowane wybranym specjalizacjom medycznym, wydaje książki oraz prowadzi portale o tematyce medycznej.
Wydawnictwo medyczne Cornetis publikuje czasopisma dedykowane wybranym specjalizacjom medycznym, wydaje książki oraz prowadzi portale o tematyce medycznej.
DNA-dependent protein kinase (DNA-PK) consists of a 460 kDa subunit that contains the catalytic domain (DNA-PKcs) complexed with two polypeptides of 70 kDa and 80 kDa (Ku70 and Ku80) which comprise the Ku autoantigen. DNA-PKcs requires association with DNA via Ku for catalytic activation and is implicated in double strand break repair, V(D)J recombination and transcription. We have utilised a cell-free system of concentrated Xenopus laevis egg extracts to investigate the regulation and possible functions of DNA-PK. Recently, we have shown that this system can reproduce events of apoptosis, including activation of an apoptotic protease that cleaves poly(ADP-ribose) polymerase. Here, we report that DNA-PK is rapidly inactivated with the onset of apoptosis in this system. Loss of activity is concomitant with cleavage of the catalytic subunit, whereas the Ku subunits are stable. Cleavage and inactivation of DNA-PKcs is prevented by prior addition of the anti-apoptotic protein Bcl-2 or inhibition of ...
The catalytic domain of glucoamylases G1 and G2 from Aspergillus niger is produced in vitro in high yield by limited proteolysis using either subtilisin Novo or subtilisin Carlsberg. Purification by affinity chromatography on an acarbose-Sepharose column followed by ion-exchange chromatography on HiLoad Q-Sepharose leads to separation of a number of structurally closely related forms of domain. The cleavage occurs primarily between Val-470 and Ala-471 as indicated by C-terminal sequencing, whereas the N-terminus is intact. Subtilisin Carlsberg, in addition, produces a type of domain which is hydrolysed before Ser-444, an O-glycosylated residue. This leaves the fragment Ser-444-Val-470 disulphide-bonded to the large N-terminal part of the catalytic domain. Subtilisin Novo, in contrast, tends to yield a minor fraction of forms extending approx. 30-40 amino-acid residues beyond Val-470. The thermostability is essentially the same for the single-chain catalytic domain and the original glucoamylases ...
Mono- and Stereopictres of 5.0 Angstrom coordination sphere of Iron atom in PDB 3pah: Human Phenylalanine Hydroxylase Catalytic Domain Dimer With Bound Adrenaline Inhibitor
Sedolisins (serine-carboxyl peptidases) are proteolytic enzymes whose fold resembles that of subtilisin; however, they are considerably larger, with the mature catalytic domains containing approximately 375 amino acids. The defining features of these enzymes are a unique catalytic triad, Ser-Glu-Asp, as well as the presence of an aspartic acid residue in the oxyanion hole. High-resolution crystal structures have now been solved for sedolisin from Pseudomonas sp. 101, as well as for kumamolisin from a thermophilic bacterium, Bacillus novo sp. MN-32. The availability of these crystal structures enabled us to model the structure of mammalian CLN2, an enzyme which, when mutated in humans, leads to a fatal neurodegenerative disease. This review compares the structural and enzymatic properties of this newly defined MEROPS family of peptidases, S53, and introduces their new nomenclature ...
Hydrogenases catalyze the formation of hydrogen. The cofactor (H-cluster) of [FeFe]-hydrogenases consists of a [4Fe-4S] cluster bridged to a unique [2Fe] subcluster whose biosynthesis in vivo requires hydrogenase-specific maturases. Here we show that a chemical mimic of the [2Fe] subcluster can reconstitute apo-hydrogenase to full activity, independent of helper proteins. The assembled H-cluster is virtually indistinguishable from the native cofactor. This procedure will be a powerful tool for developing new artificial H-2-producing catalysts.. ...
An entry from the Cambridge Structural Database, the worlds repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures ...
An entry from the Cambridge Structural Database, the worlds repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures ...
The plot of fractional enzyme activity versus extent of protein modification, for cases where all enzyme modifiable groups of a certain kind are essential for activity, is found to be nearly independent of the number, per enzyme active site, of modifiable groups involved. Such plots usually, by a fallacious extension of the initial portion of the plot on the extent-of-modification axis, are interpreted to mean the modification of one single group per enzyme active site (or per enzyme molecule). The possible relevance of these findings to cases in the literature is discussed.. ...
NQO1 is a FAD containing NAD(P)H-dependent oxidoreductase that catalyzes the reduction of quinones and related substrates. In cells, NQO1 participates in a number of binding interactions with other proteins and mRNA and these interactions may be influenced by the concentrations of reduced pyridine nucleotides. NAD(P)H can protect NQO1 from proteolytic digestion suggesting that binding of reduced pyridine nucleotides results in a change in NQO1 structure. We have used purified NQO1 to demonstrate the addition of NAD(P)H induces a change in the structure of NQO1; this results in the loss of immunoreactivity to antibodies that bind to the C-terminal domain and to helix 7 of the catalytic core domain ...
COVER The enzymes that catalyze fatty acid formation are large protein complexes with multiple active sites. The architecture of the mammalian multienzyme (catalytic domains in various colors) is quite different from that of the fungal fatty acid synthase (in gray). Nonetheless, they catalyze the same conserved reaction pathway. See pages 1258 and 1263. Image: S. Jenni and T. Maier ...
Active site of hexosaminidases with dockedpNP-GlcNAc-sulfate 6. Active site of hexosaminidases with docked pNP-GlcNAc-sulfate 6 after molecular dynamics simulat
Infection, Interferon, Kinase, Lung, RNA, Cellulose, Cellobiohydrolase, Trichoderma, Ability, Catalytic Domain, Polymers, Polymer, Production, Transfer, and Chemistry
In the past three months, maca root has provided the key active ingredient in several new European skin care brands, including the Body Shops new range for men.
In the past three months, maca root has provided the key active ingredient in several new European skin care brands, including the Body Shops new range for men.
CYP1A1 was one of the first P450 enzymes to be characterised and, as its name indicates, holds the first place in the systematic nomenclature of P450s [1]. However, it was not until last year that the first crystal structure of human CYP1A1 in complex with α-naphthoflavone has been determined at 2.6 Å resolution [2]. The structure [3] is released this week. ...
Human 5-AMP-activated protein kinase catalytic subunit alpha-2 (PRKAA2) ELISA Kit can measure Human 5-AMP-activated protein kinase catalytic subunit alpha-2 in serum, blood, plasma, cell culture supernatant and other related supernatants and tissues.
... domain; an α-helical membrane-binding moiety; and a C-terminal catalytic domain. PTGS (COX, which can be confused with " ... The catalytic domain is homologous to mammalian peroxidases such as myeloperoxidase.[24][25] ... Both the cyclooxygenase and the peroxidase active sites are located in the catalytic domain, which accounts for approximately ... It has been found that human PTGS2 (COX-2) functions as a conformational heterodimer having a catalytic monomer (E-cat) and an ...
This enzyme has 8 helical domains anchoring it in the Golgi membrane of the ER; the catalytic domain is in the cytosol. It is ...
A C-terminal catalytic domain (residues 126-673). *An N-terminal C2-like domain which promotes its binding to ligand substrates ... A PLAT domain within its C2-like domain; this domain, by analogy to other PLAT domain-bearing proteins, may serve as a mobile ... A proline-rich region (residues 566-577), sometimes termed a SH3-binding domain, which promotes its binding to proteins with ... The enzyme possesses two catalytic activities as illustrated by its metabolism of arachidonic acid. ALOX5's dioxygenase ...
Cleavage of C99 within its transmembrane domain by γ-secretase releases the intracellular domain of APP and produces amyloid-β ... The transmembrane protein contains two active site aspartate residues in its extracellular protein domain and may function as a ... 1sgz: Crystal Structure of Unbound Beta-Secretase Catalytic Domain. *. 1tqf: Crystal structure of human Beta secretase ...
... from rat showing two of its domains, the tetramerization domain (pink) and the catalytic domain (blue). ... As for the tetramerization and catalytic domains their structure was found with rat tyrosine hydroxylase using X-ray ... protein domain specific binding. Cellular component. • cytoplasm. • cytosol. • mitochondrion. • neuron projection. • ... At the carboxyl terminal of the peptide chain there's a short alpha helix domain that allows tetramerization.[15] The central ~ ...
... and the calcium ion are present in the catalytic domain approximately 12 Å away from the catalytic zinc. The catalytic zinc ion ... a catalytic domain; and a hemopexin-like domain at the carboxy-terminal. The propeptide consists of approximately 80-90 amino ... The catalytic domain contains two zinc ions and at least one calcium ion coordinated to various residues. One of the two zinc ... The catalytic domain of MMP-3 can be inhibited by tissue inhibitors of metalloproteinases (TIMPs). The n-terminal fragment of ...
1elv: CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN COMPLEMENT C1S PROTEASE ... Rossi V, Gaboriaud C, Lacroix M, Ulrich J, Fontecilla-Camps JC, Gagnon J, Arlaud GJ (June 1995). "Structure of the catalytic ... Busby TF, Ingham KC (May 1990). "NH2-terminal calcium-binding domain of human complement C1s- mediates the interaction of C1r- ... 1nzi: Crystal Structure of the CUB1-EGF Interaction Domain of Complement Protease C1s ...
The nucleotide exchange occurs at the catalytic Sec7 domain of GBF1. Activated Arf1p then recruits coat protein β-COP, a ...
... domain; an α-helical membrane-binding moiety; and a C-terminal catalytic domain. PTGS (COX, which can be confused with " ... The catalytic domain is homologous to mammalian peroxidases such as myeloperoxidase. It has been found that human PTGS2 (COX-2 ... Both the cyclooxygenase and the peroxidase active sites are located in the catalytic domain, which accounts for approximately ... Each subunit has three different structural domains: a short N-terminal epidermal growth factor (EGF) ...
... the catalytic domain (residues 153-425); and the C-terminal domain (residues 426-692), which is further divided into three ... A number of monoclonal antibodies that bind to and inhibit PCSK9 near the catalytic domain were in clinical trials as of 2014[ ... though the N-terminal prodomain retains its association with the catalytic domain. In particular, residues 61-70 in the N- ... domain of the LDLR. While previous studies indicated that the C-terminal domain was uninvolved in binding LDLR, a recent study ...
Antiparallel orientation of the catalytic domains". J. Biol. Chem. 275 (52): 41476-86. doi:10.1074/jbc.M007480200. PMID ...
It has four functional domains, including an N-terminal domain, a highly conserved catalytic (HAT) domain, an Ada2 interaction ... Relative sizes and locations of important domains for representative HATs (HAT = catalytic acetyltransferase domain; Bromo = ... p300/CBP are metazoan-specific[6] and contain several zinc finger regions, a bromodomain, a catalytic (HAT) domain, and regions ... On a broader scale, the structures of the catalytic domains of GNAT proteins (Gcn5, PCAF) exhibit a mixed α/β globular fold ...
"Peptidylglycine alpha-amidating monooxygenase: a multifunctional protein with catalytic, processing, and routing domains" ... The HIFalpha prolyl hydroxylases, termed PHDs/EGLNs (prolyl hydroxylase domain proteins/EGL nine homologues), bind to a ...
"Peptidylglycine alpha-amidating monooxygenase: a multifunctional protein with catalytic, processing, and routing domains" ...
DAG-kinase catalytic (DAGKc) domain in PROSITE. ...
HDAC10 has two catalytic domains as well. One active domain is located in the N-terminus and a putative catalytic domain is ... However, HDAC6's catalytic domain is most similar to HDAC9. A unique feature of HDAC6 is that it contains two catalytic domains ... 5 and 7 have their catalytic domains located in the C-terminus along with an NLS region while HDAC9 has its catalytic domain ... domain with a HAT domain in-between. The last is TAFII250 which has a Kinase domain at the N-terminus region, two bromodomains ...
2oc3: Crystal Structure of the Catalytic Domain of Human Protein Tyrosine Phosphatase non-receptor Type 18 ... This PTP contains a PEST motif, which often serves as a protein-protein interaction domain, and may be related to protein ... "SH2 Domain-Mediated Interaction of Inhibitory Protein Tyrosine Kinase Csk with Protein Tyrosine Phosphatase-HSCF". Mol. Cell. ...
The related catalytic domains of Deiodinases 1-3 feature a thioredoxine-related peroxiredoxin fold. The enzymes catalyze a ... "Crystal structure of mammalian selenocysteine-dependent iodothyronine deiodinase suggests a peroxiredoxin-like catalytic ... "Crystal structure of mammalian selenocysteine-dependent iodothyronine deiodinase suggests a peroxiredoxin-like catalytic ...
The V1 domain contains the ATP catalytic site. The protein encoded by this gene is one of two V1 domain B subunit isoforms and ... V-ATPase is composed of a cytosolic V1 domain and a transmembrane V0 domain. The V1 domain consists of three A, three B, and ...
The membrane-bound form has both membrane-binding and catalytic domains. The soluble form has only the catalytic domain. This ... Exon 2 contains the junction of the membrane-binding domain and the catalytic domain of b5R, which shows that there are two ... this isoform has one hydrophobic membrane-anchoring domain and one catalytic domain that is hydrophilic. The other isoform, a ... The NH2-terminal structure of the membrane-binding domain is CH3(CH2)12-CO-Gly-Ala-Gln-Leu-Ser-Thr-Leu-Gly-His-Met-Val-Leu-Phe- ...
The V1 domain contains the ATP catalytic site. The V0 domain consists of five different subunits: a, c, c', c", and d. ... V-ATPase is composed of a cytosolic V1 domain and a transmembrane V0 domain. The V1 domain consists of three A and three B ... This encoded protein is part of the V0 domain. This gene had the previous symbols of ATP6C and ATP6L. GRCh38: Ensembl release ...
The V1 domain contains the ATP catalytic site. The V0 domain consists of five different subunits: a, c, c', c, and d. ... V-ATPase is composed of a cytosolic V1 domain and a transmembrane V0 domain. The V1 domain consists of three A and three B ...
The V1 domain contains the ATP catalytic site. The V0 domain consists of five different subunits: a, c, c', c", and d. ... V-ATPase is composed of a cytosolic V1 domain and a transmembrane V0 domain. The V1 domain consists of three A and three B ... 2002). "The amino-terminal domain of the E subunit of vacuolar H(+)-ATPase (V-ATPase) interacts with the H subunit and is ...
The V1 domain contains the ATP catalytic site. This gene encodes alternate transcriptional splice variants, encoding different ... V-ATPase is composed of a cytosolic V1 domain and a transmembrane V0 domain. The V1 domain consists of three A, three B, and ... 2000). "The B1 subunit of the H+ATPase is a PDZ domain-binding protein. Colocalization with NHE-RF in renal B-intercalated ... V1 domain E subunit isoforms. Pseudogenes for this gene have been found in the genome. GRCh38: Ensembl release 89: ...
The V1 domain contains the ATP catalytic site. The V0 domain consists of five different subunits: a, c, c', c", and d. ... V-ATPase is composed of a cytosolic V1 domain and a transmembrane V0 domain. The V1 domain consists of three A and three B ... This gene encodes the regulatory H subunit of the V1 domain which is required for catalysis of ATP but not the assembly of V- ... Lu M, Vergara S, Zhang L, Holliday LS, Aris J, Gluck SL (Oct 2002). "The amino-terminal domain of the E subunit of vacuolar H ...
The V1 domain contains the ATP catalytic site. The V0 domain consists of five different subunits: a, c, c', c, and d. ... V-ATPase is composed of a cytosolic V1 domain and a transmembrane V0 domain. The V1 domain consists of three A and three B ... This encoded protein is one of two V1 domain B subunit isoforms and is found in the kidney. Mutations in this gene cause distal ...
PDZ domain binding. • cadherin binding. • peptidase activity. • beta-catenin binding. • protein binding. • calcium channel ... positive regulation of catalytic activity. • mitochondrial transport. • post-embryonic development. • positive regulation of ... Presenilin possesses a 9 transmembrane domain topology, with an extracellular C-terminus and a cytosolic N-terminus.[7][8] ... membrane protein intracellular domain proteolysis. • positive regulation of protein import into nucleus. • ephrin receptor ...
The V1 domain contains the ATP catalytic site. This gene encodes alternate transcriptional splice variants, encoding different ... V-ATPase is composed of a cytosolic V1 domain and a transmembrane V0 domain. The V1 domain consists of three A,three B, and two ... V1 domain C subunit isoforms. GRCh38: Ensembl release 89: ENSG00000143882 - Ensembl, May 2017 GRCm38: Ensembl release 89: ...
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites ... Domain relationships *Phosphatidylinositol 3-/4-kinase, catalytic domain (IPR000403) *PI3Kalpha, catalytic domain (IPR037704) ... Protein kinase-like domain superfamily (IPR011009). *Phosphatidylinositol 3-/4-kinase, catalytic domain superfamily (IPR036940) ... a Ras binding domain, a lipid binding C2 domain, a PI3K homology domain of unknown function, and a C-terminal ATP-binding ...
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites ... Domain relationships *Peptidase family A1 domain (IPR033121) *Aspergillopepsin-like catalytic domain (IPR034163) ... Aspergillopepsin-like catalytic domain (IPR034163). Short name: Aspergillopepsin-like_cat_dom Overlapping homologous ... The N- and C-terminal domains, although structurally related by a 2-fold axis, have only limited sequence homology except the ...
alpha amylase, catalytic domain protein [Capnocytophaga sp. oral taxon 380 str. F0488]. NCBI Reference Sequence: ZP_19279919.1 ... Identify Conserved Domains View conserved domains detected in this protein sequence using CD-search. ...
CAMP-SPECIFIC 3,5-CYCLIC PHOSPHODIESTERASE 4D1,2-Ethanediol2-[3-(2-Hydroxy-1,1-Dihydroxymethyl-Ethylamino)-Propylamino]-2-Hydroxymethyl-Propane-1,3-DiolAdenosine Monophosphate
Dot1 is an evolutionarily conserved histone methyltransferase that methylates lysine-79 of histone H3 in the core domain. ... Unlike other histone methyltransferases, Dot1 does not contain a SET domain, and it specifically methylates nucleosomal histone ... Structure of the catalytic domain of human Dot1L, a non-SET domain nucleosomal histone methyltransferase. *Min J ... Min, J., Feng, Q., Li, Z., Zhang, Y., & Xu, R. M. (2003). Structure of the catalytic domain of human Dot1L, a non-SET domain ...
... the catalytic domain remains either undetermined or ambiguous. Characterization of the catalytic domain in these superfamilies ... The catalytic domain of all eukaryotic cut-and-paste transposase superfamilies Message Subject (Your Name) has sent you a ... The catalytic domain of all eukaryotic cut-and-paste transposase superfamilies. Yao-Wu Yuan and Susan R. Wessler ... A catalytic domain signified by an acidic amino acid triad, known as the "DDE/D" motif, has been unambiguously identified in ...
Catalytic domain (ab65911). Please let us know if you have used this product in your publication ...
Crystal structures of the catalytic domain of HIV-1 integrase free and complexed with its metal cofactor: high level of ... Fragment: CATALYTIC CORE DOMAIN 50 - 212 Mutation: F185H Gene Name(s): gag-pol ...
... the catalytic domain of bacteriophage HP1 integrase at 2.7 A resolution. ... Domain Info. Class. Fold. Superfamily. Family. Domain. Species. A. d1aiha_. Alpha and beta proteins (a+b) DNA breaking- ... Domain Annotation: CATH CATH Database (version 4.0.0) Homepage. Chains. Domain. Class. Architecture. Topology. Homology. ... Lambda integrase-like, catalytic core Integrase Bacteriophage HP1 [TaxId: 10690] B. d1aihb_. Alpha and beta proteins (a+b) DNA ...
Catalytic domain used in Immunocytochemistry/ Immunofluorescence. Abcam provides excellent in-house scientific support ...
... catalytic domain include The Multifaceted Benefits of Protein Co-expression in Escherichia coli, Using Scaffold Liposomes ... Catalytic Domain: The region of an enzyme that interacts with its substrate to cause the enzymatic reaction. The Multifaceted ...
GC-A contains an ANF-binding domain in the extracellular region and a kinase-like domain and catalytic domain in the ... catalytic domain).4 Since the catalytic domain of guanylate cyclase (GC-c) can be functionally expressed as a soluble protein ... The catalytic domain plus a portion of the kinase-like domain of GC-A (293 amino acids) have been expressed in Escherichia coli ... Recently, we have further shown that the catalytic domain plus three amino acids from the kinase-like domain of GC-A (242 amino ...
Chimeric Proteins Suggest That the Catalytic and/or C-Terminal Domains Give CesA1 and CesA3 Access to Their Specific Sites in ... Dimerization of cotton fiber cellulose synthase catalytic subunits occurs via oxidation of the zinc-binding domains. Isaac ... Lack of activation of the two-hybrid system by the Zn domain fused to the GAL4 activating domain (Fig. 2A, 4 and 5) further ... As for the yeast two-hybrid system, this domain of CesA1 can interact with itself (Fig. 2B, lane 5) or with the similar domain ...
Following domains in our database have detailed information on amino acids needed for their catalytic activity. When any of ... these domains appear in the sequences analyzed, the domain annotation pages will show a detailed report on the catalytic ...
Computer model showing the structure of the catalytic domain of eukaryotic guanylate cyclase (green, blue). PO4 residues shown ... Caption: Catalytic domain of eukaryotic guanylate cyclase. Computer model showing the structure of the catalytic domain of ... Keywords: art, artwork, biochemical, biochemistry, biological, biology, black background, catalytic, compound, cyclase, ...
Phylogenetic mapping of the conserved protein kinase catalytic domains can serve as a useful first step in the functional ... The protein kinase family: conserved features and deduced phylogeny of the catalytic domains ... The protein kinase family: conserved features and deduced phylogeny of the catalytic domains ... The protein kinase family: conserved features and deduced phylogeny of the catalytic domains ...
... catalytic domain superfamily including the families contained in it. Additional information provided includes InterPro ... annotation (if available), Functional annotation, and SUPERFAMILY links to genome assignments, alignments, domain combinations ... Metalloproteases ("zincins"), catalytic domain superfamily. SCOP classification Root: SCOP hierarchy in SUPERFAMILY [. 0] (11) ... There are 56 hidden Markov models representing the Metalloproteases ("zincins"), catalytic domain superfamily. Information on ...
the catalytic domain is very similar to that of the bacterial beta-amylase; but contains a typical alpha-amylase extra domain * ... in alpha-amylases and closer relatives this domain is usually followed by a common all-beta domain Protein Domains:. *Bacterial ... Family: Amylase, catalytic domain. members of the family may contain various insert subdomains. in alpha-amylases and closer ... protein shares similar domain organization with maltogenic amylases but differs in the spatial arrangement of its domains * ...
The protein kinase family: conserved features and deduced phylogeny of the catalytic domains ... The protein kinase family: conserved features and deduced phylogeny of the catalytic domains ... The protein kinase family: conserved features and deduced phylogeny of the catalytic domains ... The protein kinase family: conserved features and deduced phylogeny of the catalytic domains ...
Since this product is a truncated protein and does not contain intracellular catalytic activity domain, it is not suitable for ... PDGFRA Recombinant Human Protein (without Catalytic Activity Domain), His Tag, Invitrogen™ Sino Biological™ 50ug ... PDGFRA Recombinant Human Protein (without Catalytic Activity Domain), His Tag, Invitrogen™ Sino Biological™ ... This recombinant protein was expressed from a DNA sequence encoding the extracellular domain (Met 1-Glu 524) of human PDGFRA ( ...
Inhibition of human HGK catalytic domain expressed in baculovirus assessed as substrate phosphorylation using fluorescence- ...
It is established that the catalytic domain of PCSK9 (aa153-421) and the EGF-A domain of LDL-R (aa314-355) are involved in the ... LDL-R promoting activity of peptides derived from human PCSK9 catalytic domain (153-421): design, synthesis and biochemical ... The major goal of this study is to identify peptide/s from the catalytic domain of hPCSK9 that can block the binding of hPCSK9 ... It is proposed that LDL-R promoting activity of this and other selected PCSK9 catalytic peptides such as P36, P37, P46 and P47 ...
... catalytic domain was isolated from a fungal highly reducing iterative polyketide synthase (HR-iPKS) for the first time and ... A cis-acting enoyl reductase (ER) catalytic domain was isolated from a fungal highly reducing iterative polyketide synthase (HR ... Substrate selectivity of an isolated enoyl reductase catalytic domain from an iterative highly reducing fungal polyketide ... Substrate selectivity of an isolated enoyl reductase catalytic domain from an iterative highly reducing fungal polyketide ...
Inhibition of human FGFR2 N549H mutant catalytic domain expressed in baculovirus assessed as substrate phosphorylation using ...
The novel mutation is located in the catalytic domain, as are 3 (p.E404K, p.V400del and p.G406D) of the other 13 MMP2 mutations ... By protein modelling, the mutant residue was predicted to affect the main chain conformation of the catalytic domain. Gelatin ... Functional characterisation of a novel mutation affecting the catalytic domain of MMP2 in siblings with multicentric osteolysis ... broaden the repertoire of reported MMP2 mutation and enhance the comprehension of the protein motifs crucial for MMP2 catalytic ...
  • Except for a few members of the CslD family, the closest ancestors to the CesA genes and some of which may function in cellulose synthesis in tip-growing cells, these domains are notably lacking in the other members of the CesA superfamily ( 3 , 19 ). (pnas.org)
  • Three-dimensional modeling of the I-TevI homing endonuclease catalytic domain, a GIY-YIG superfamily member, using NMR restraints and Monte Carlo dynamics. (dbcls.jp)
  • We recently demonstrated that amino acid 119, in the α2 helix of the central domain of the human immunodeficiency virus type 1 integrase, affected the choice of nonviral target DNA sites. (asm.org)
  • Studies using chimeric integrases involving human immunodeficiency virus type 1 (HIV-1), feline immunodeficiency virus, and visna virus indicate that the central domain of integrase plays a major role in selecting the target sites for insertion of viral DNA ends. (asm.org)
  • The crystal structure and biochemical properties of the C-terminal catalytic domain of SSV1 integrase, an archaeal member of the tyrosine recombinase family, are described. (iucr.org)
  • One notable characteristic of all of the CesA proteins is the presence of two zinc-finger domains located within the cytoplasmic N-terminal region of the proteins. (pnas.org)
  • We studied hTERT proteins containing N-terminal deletions or substitutions to identify and characterize hTERT domains mediating telomerase catalytic activity, hTR binding, and hTERT multimerization. (asm.org)
  • This discovery was significant, as many SET domain proteins had been identified as transcriptional regulators, but their mode of action was not understood. (embopress.org)
  • OXR1 contains the Tre2/Bub2/Cdc16 (TBC), lysin motif (LysM), domain catalytic (TLDc) domain, a motif present in a family of proteins including TBC1 domain family member 24 (TBC1D24), a protein mutated in a range of disorders characterized by seizures, hearing loss, and neurodegeneration. (ox.ac.uk)
  • To understand the role of this domain in the stress response, we carried out systematic analysis of all mammalian TLDc domain-containing proteins, investigating their expression and neuroprotective properties in parallel. (ox.ac.uk)
  • Our data demonstrate that the integrity of the TLDc domain is essential for conferring neuroprotection, an important step in understanding the functional significance of all TLDc domain-containing proteins in the cellular stress response and disease. (ox.ac.uk)
  • Cytosolic adaptor proteins (APs), which recognize the cytosolic domains of proteins that span the SG membrane, have been shown to play essential roles in the assembly of functional SGs. (frontiersin.org)
  • Functional characterisation of a novel mutation affecting the catalytic domain of MMP2 in siblings with multicentric osteolysis, nodulosis and arthropathy. (sigmaaldrich.com)
  • Our results further delineate the complexity of genotype-phenotype correlations in MONA, broaden the repertoire of reported MMP2 mutation and enhance the comprehension of the protein motifs crucial for MMP2 catalytic activity. (sigmaaldrich.com)
  • We have previously found that a valine-to-isoleucine point mutation at position 157 (V157I mutant) within the tyrosine kinase domain of this truncated erbB can dramatically activate the sarcomagenic potential of the oncogene and increase the kinase activity of this oncoprotein. (elsevier.com)
  • View conserved domains detected in this protein sequence using CD-search. (nih.gov)
  • The major obstacle is that the catalytic domain of GC-A does not contain G-x-G-x-x-G, the diagnostic consensus sequence of the nucleotide binding site that interacts with the phosphate chain of the nucleotide. (ahajournals.org)
  • It is expected that sequence of the ancestor PTP catalytic domain and its characteristics will consistently contribute to our understanding of the evolution of PTPs and the physiological function of the ancestor PTP. (biochim.ro)
  • On the basis of this analogy, molecular modeling studies of epsilon186 were performed using as templates the crystal structures of the exonuclease domains of the Klenow fragment and the T4 DNA polymerase and the recently determined structure of the E. coli Exonuclease I. A multiple sequence alignment was constructed, with the initial alignment taken from the previously published hidden Markov model and NMR constraints. (neb.com)
  • The catalytic units of Ser/Thr protein phosphatases 1, 2A and 2B (PP1c, PP2Ac and PP2Bc, respectively), which exhibit about 45% sequence similarity, have their active centers practically identical. (edu.pl)
  • The hemopexin-like domain of MMPs is highly conserved and shows sequence similarity to the plasma protein, hemopexin. (wikipedia.org)
  • The binding affinity of PDE6 for pharmacological inhibitors or for the C-terminal region of the inhibitory gamma subunit (Pgamma), known to directly inhibit PDE6 catalysis, was increased approximately 2-fold by ligands binding to the GAF domain. (unh.edu)
  • The catalytic subunit responsible for glucan chain elongation is believed to be a plasma membrane glycosyltransferase named CesA (cellulose synthase). (pnas.org)
  • Our results suggest that functional hTERT complementation requires intact RID2 and RT domains on the same hTERT molecule and is dependent on hTR and the N terminus. (asm.org)
  • The catalytic subunit of ISW2 consists of the ATPase domain and three domains at the C-terminus called HAND, SANT and SLIDE (HSS) domains. (siu.edu)
  • In summary, the understandings of Isw2 ATPase domain and C-terminus domains support the assumption that there is no redundancy of their roles in nucleosome remodeling. (siu.edu)
  • Mapping of the catalytic and epitopic sites of human CD38/NAD+ glycohydrolase to a functional domain in the carboxyl terminus. (semanticscholar.org)
  • Human SENP1 (catalytic domain aa 387-644) (Accession Nr. Q9P0U3 ) fused at the N-terminus to a His-tag. (adipogen.com)
  • GC search motifs constructed from the alignment of known GCs catalytic centers form vertebrates and lower eukaryotes have led to the identification of a number of plant GCs that have been characterized in vitro and in vivo . (biomedcentral.com)
  • 40) of multi-domain molecules with potentially functional GC catalytic centers in plants that remain to be discovered and characterized. (biomedcentral.com)
  • Theoretical models of catalytic domains of protein phosphatases 1 and 2A with Zn2+ and Mn2+ metal dications and putative bioligands in their catalytic centers. (edu.pl)
  • Although Zn 2+ binding occurs only when the protein is in the reduced form, biochemical analyses show that under oxidative conditions, the GhCesA1 zinc-finger domain and also the full-length protein dimerize via intermolecular disulfide bonds, indicating CesA dimerization can be regulated by redox state. (pnas.org)
  • Several conserved domains of the CesA protein orthologs have been characterized (illustrated schematically in Fig. 1B ). (plantphysiol.org)
  • This configuration is in stark contrast to the domain organization obtained in predicted structures of plant CesA. (plantcell.org)
  • We also provide evidence that the herbicide CGA 325′615 (Syngenta, Basel), which inhibits synthesis of crystalline cellulose and leads to a disruption of rosette architecture, may affect the oxidative state of the zinc-finger domain that is necessary for rosette stability. (pnas.org)
  • 3 4 However, although the catalytic domain of GC-A has been assigned to a 239-amino acid region, 4 the exact location of the active site (or the catalytic cavity) is still unknown. (ahajournals.org)
  • It is necessary to have at least a dimer for creation of the catalytic cavity. (jbsdonline.com)
  • We propose in this project to reconstruct and characterize the catalytic domain of an ancestor of RPTPs. (biochim.ro)
  • This leaves the fragment Ser-444-Val-470 disulphide-bonded to the large N-terminal part of the catalytic domain. (biochemj.org)
  • This entry represents the peptidase domain found in a group of aspartic endopeptidases of fungal origin, including aspergillopepsin (MEROPS ientifier A01.016) [ PMID: 11418762 ], rhizopuspepsin (A01.012), endothiapepsin (A01.017) and penicillopepsin (A01.011) [ PMID: 339694 ]. (ebi.ac.uk)
  • This entry represents the catalytic domain of PI3Kalpha (also known as p110alpha), which is a Class IA phosphoinositide-3-kinase (PI3K) that that phosphorylates PtdIns (Phosphatidylinositol), PtdIns4P (Phosphatidylinositol 4-phosphate) and PtdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). (ebi.ac.uk)
  • In addition, prolonged incubation of PDE6 with vardenafil or sildenafil (but not 3-isobutyl-1-methylxanthine and zaprinast) induced a distinct conformational change in the catalytic domain without affecting the binding properties of the GAF domains. (unh.edu)
  • Furthermore, we have elucidated the thermodynamic and conformational cycle of the helicase-like domain, and predicted the stages fulfilling the requirements for interdomain communication, local duplex DNA unwinding, and the stages where DNA is in a suitable state to support the supercoiling reaction. (unibas.ch)
  • Finally, besides the use of smFRET as a tool to investigate conformational changes in solution, we have also provided high-resolution snapshots of the helicase-like domain via X-ray crystallography. (unibas.ch)
  • Additionally, we also elucidated the nucleotide cycle and conformational transitions for this helicase-like domain mutant, which gave the first indications of why no positive supercoiling can be performed by the full-length reverse gyrase lacking the latch, and only DNA relaxation is allowed. (unibas.ch)
  • However, when PCSK9 binds to the LDLR (through the EGF-A domain), PCSK9 prevents the conformational change of the receptor-ligand complex. (wikipedia.org)
  • A cis -acting enoyl reductase (ER) catalytic domain was isolated from a fungal highly reducing iterative polyketide synthase (HR-iPKS) for the first time and studied in vitro . (rsc.org)
  • The catalytic domain of glucoamylases G1 and G2 from Aspergillus niger is produced in vitro in high yield by limited proteolysis using either subtilisin Novo or subtilisin Carlsberg. (biochemj.org)
  • We identified two RNA interaction domains, RID1 and RID2, the latter containing a vertebrate-specific RNA binding motif. (asm.org)
  • The JmjC domain is a double-stranded β-helical (DSBH) fold also called the jelly-roll fold or double Greek motif. (nih.gov)
  • The Evolutionarily Conserved Tre2/Bub2/Cdc16 (TBC), Lysin Motif (LysM), Domain Catalytic (TLDc) Domain Is Neuroprotective against Oxidative Stress. (ox.ac.uk)
  • Although both Csk and MAP kinases used docking sites for substrate recognition, their docking sites consisted of different substructures in the catalytic domain. (elsevier.com)
  • C) Catalytic core of human methyladenosine demethylase FTO (PDB ID: 3LFM ) demonstrating the double-stranded β-helical fold and including the active site metal (blue sphere). (nih.gov)
  • SENP1 (catalytic domain) (human) (rec. (adipogen.com)
  • Insights into the regulation of the human COP9 signalosome catalytic subunit, CSN5/Jab1. (biomedsearch.com)
  • Avian c-erbB is activated to a leukemia oncogene following truncation of its amino-terminal ligand-binding domain by retroviral insertion. (elsevier.com)
  • The thermostability is essentially the same for the single-chain catalytic domain and the original glucoamylases G1 and G2, whereas the catalytic domain cut between Ser-443 and Ser-444 is less thermostable. (biochemj.org)
  • The transposases from several superfamilies possess a protein domain containing an acidic amino acid triad (DDE or DDD) that catalyzes the "cut and paste" transposition reaction. (pnas.org)
  • However, it was unclear whether this domain was shared by the transposases from all superfamilies. (pnas.org)
  • The overall fold of the catalytic JmjC domain in iron- and 2-oxoglutarate-dependent histone demethylases and nucleotide hydroxylases(A) Jmj prototype member JmjD2A (PDB ID: 2OQ7) in complex with Ni2+ (which replaces the endogenous Fe2+) and the 2-oxoglutarate competitive inhibitor N-oxalyl glycine (NOG). (nih.gov)
  • Pgamma1-60 binding to the GAF domain increased vardenafil but not cGMP affinity, indicating that substrate- and inhibitor-binding sites do not totally overlap. (unh.edu)