Polymerase structure: Co(III)bleomycinB2 bithiazole/C-terminal tail domain bound to d(ATTTAGTTAACTAAAT) complexed with MMLV RT catalytic fragment ( PDBid: 2R2U)
Protein domains are compact regions of a proteins structure that often convey some distinct function. Domain architecture, or order of domains in a protein, is frequently considered as a fundamental level of protein functional complexity [1]. The majority of the protein repertoire is composed of multidomain proteins; two-thirds of the proteins in prokaryotes and about four-fifths eukaryotic ones have two or more domains [2]. Moreover, an organisms complexity relates much better to the number of distinct domain architectures [3] and expansion in particular domain families [4] than to the number of genes in the organism. The prevalence of proteins with more than two domains and the recurrent appearance of the same domain in non-homologues proteins show that functional domains are reused when creating new proteins. Because of this, domains have been likened to Lego bricks that can be recombined in various ways to build proteins with completely new functions [5]. Hence, one way to study evolution ...
The sterile alpha motif (SAM) is a protein interaction domain of around 70 amino acids present predominantly in the N- and C-termini of more than 60 diverse proteins that participate in signal transduction and transcriptional repression. SAM domains have been shown to homo- and hetero-oligomerize and to mediate specific protein-protein interactions. A highly conserved subclass of SAM domains is present at the intracellular C-terminus of more than 40 Eph receptor tyrosine kinases that are involved in the control of axonal pathfinding upon ephrin-induced oligomerization and activation in the event of cell-cell contacts. These SAM domains appear to participate in downstream signaling events via interactions with cytosolic proteins. We determined the solution structure of the EphB2 receptor SAM domain and studied its association behavior. The structure consists of five helices forming a compact structure without binding pockets or exposed conserved aromatic residues. Concentration-dependent chemical ...
The SCOP classification for the Signal peptide-binding 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, taxonomic visualisation and hidden Markov model information.
(2004) Luoni et al. FEBS Letters. Type IIB Ca2+-ATPases have a terminal auto-inhibitory, domain the action of which is suppressed by calmodulin (CaM) binding. Here, we show that a peptide (6His-1M-I116) corresponding to the first 116 aminoacids (aa) of At-ACA8, the first cloned isoform of Arabido...
Shop KH homology domain-containing protein ELISA Kit, Recombinant Protein and KH homology domain-containing protein Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and Antibody are available.
pfam08581 (PSSM ID: 369972): Conserved Protein Domain Family Tup_N, The N-terminal domain of the Tup protein has been shown to interact with the Ssn6 transcriptional co-repressor
CSF1R protein domain and mutation schematic. Schematic diagram of the protein domain structure of CSF1R with amino acid numbers provided. Mutations previously r
pfam12756 (PSSM ID: 372293): Conserved Protein Domain Family zf-C2H2_2, This family contains two copies of a C2H2-like zinc finger domain
Shop Forkhead-associated domain-containing protein ELISA Kit, Recombinant Protein and Forkhead-associated domain-containing protein Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and Antibody are available.
Domain architectures containing both Dcp2 domain-like and Nudix in all archaea. Links to architectures containing these domain pairs in other groups of genomes are provided. Domain pairs which are not adjacent can be added/removed.
Transmembrane domain architecture, symmetry and coupling to LBDa, View of the TMD parallel to the membrane. GluN1 subunits are blue and the GluN2B subunits are
BACKGROUND: The ferlin gene family possesses a rare and identifying featureconsisting of multiple tandem C2 domains and a C-terminal transmembrane domain.Much currently remains unknown about the fundamental function of this genefamily, however, mutations in its two most well-characterised members, dysferlin and otoferlin, have been implicated in human disease. The availability of genome sequences from a wide range of species makes it possible to explore the evolutionof the ferlin family, providing contextual insight into characteristic featuresthat define the ferlin gene family in its present form in humans. RESULTS: Ferlingenes were detected from all species of representative phyla, with two ferlinsubgroups partitioned within the ferlin phylogenetic tree based on the presenceor absence of a DysF domain. Invertebrates generally possessed two ferlin genes(one with DysF and one without), with six ferlin genes in most vertebrates (threeDysF, three non-DysF). Expansion of the ferlin gene family is ...
Methods for producing and identifying fragments of proteins, and more particularly to methods for generating and identifying soluble protein domains are disclosed based on a method for generating a li
Tuning the Flexibility of Glycine-Serine Linkers ToAllow Rational Design of Multidomain Proteins Biochemistry DOI: 10.1021/acs.biochem.7b00902 More...
People Era Consulting is an emerging recruitment firm providing end to end Talent Solutions to multifarious industrial segments across the country. Our focus has always been on providing a pool of potential and validated candidates across the level i.e. Senior, Middle and Junior management. We operate through domain specialist providing high quality permanent hiring services.. ...
People Era Consulting is an emerging recruitment firm providing end to end Talent Solutions to multifarious industrial segments across the country. Our focus has always been on providing a pool of potential and validated candidates across the level i.e. Senior, Middle and Junior management. We operate through domain specialist providing high quality permanent hiring services.. ...
For domaining or for your business needs, get the best aftermarket domain names for sale today! NameJet provides premium and expiring domain names through domain auctions and backorder services.
MAADESSQNTLRLQFKAMQEMQHKRLQKQMEKKREKELSLKSRADDQEEPLEVSDGLSLLHAGEPNSKNS 1 - 70 FEKRVLEDEIEHLRNELRETVDENGRLYKLLKERDFEIKHLKKKIEEDRFAFTGTAGVAGDVVATKIVEL 71 - 140 SKKNRLLMAESEGAKTRVKQLTNRIQELERELQTALTRLSAKGATDAGAKPPRAQMGDRALLETPEVKAL 141 - 210 QDRLVATNLKMSDLRNQIQSVKQELRMAQKVLAREVGEDINVQQLLSSPGTWRGRAQQILVLQSKVQELE 211 - 280 KQLGQARSQSAGTASDELSVYPDPRKLSAQEKNLLRIRSLEREKQEGLEKLASERDVLQRELEELKKKFE 281 - 350 GMRSRNKLLSSEMKTLKSQMGTLVEKGRHDDELIDALMDQLKQLQEILGSLSLQEEKTRVSQHHLDQQLN 351 - 420 SEAQRSNSLVAQLQAMVAEREAKVRQLEMEIGQLNVHYLRNKGVGEGSSGREVSPAYTQFLEDPGLTKSP 421 - 490 ASAGDHVGRLGSSRSVTSLGHTLVESALTRPSLPSPHRTSPRFSDSPEQKGWQAQVSEIKALWQAAEVER 491 - 560 DRLTEFVTVLQKRVEESNSKLLESERKLQEERHRTVVLEQHLEKIRLEPGKASASQRAAPRTKTGLPTSN 561 - 630 NRHNPTGSEKKDPSFAQLSDVPVESQMEELTTRLAIQVEENEMLKAALGSALRGKEEDFRMYHEILGQVK 631 - 700 SVFLQALRQQKTGKQ 701 - 715 ...
MPTLVVGTPPTCLGDTPQPCHKNSQRQGPFSHGAPGRAADWKAVAKPRLCAPAAEDDVAALRWPGPSQQP 1 - 70 DPPWAAPHVVGSDDLKEPGPWGKACSLPMWSTGPEARDGDSSVSSGRLSCSSGGHDVCVSWKERPPQVLG 71 - 140 PQQRPRKSDARLEQLRDKIRAQAWQQGSCASLGTSAPSSASRLHKASTLMLRRKGQEAKNPPPAPECSGF 141 - 210 SILSAAERRVEAKASHGQGRELSRVSQHQVPVLREKPKRVKSSSCKREKTPKLPSPRRAAKDKHKDEDSE 211 - 280 LVGVYAWRKGQALVRSLLGPPPVLRRHHSKDPSRDPALTVDLGDSEKVIAAKCSPVCAQLPDATSAYSDQ 281 - 350 QVSGNTPSLASFDQPATIQTAMAILQDLRQQIQAGLELAQARKGGQELGPSKRRLQDVAGRGCCRDPNAQ 351 - 420 SSFSKSPWAMTERKHSSLERARSVHTWEPWSSSTARESCPQRAWGAQGQDRSFQRPESPHERLGHFSQRP 421 - 490 WSALAGQACSPQRAWGAQRQGPSSQRPGSPPEKRSPFPQQPWSAVATQPCPRRAWTACETWEDPGPRLRN 491 - 560 PLERPSPPAQRPWSSSGVQRAGPQGKGRGIGSPVSAAKHALPRPTGSFPQNPLGKEKDTLRPCPRSRGLL 561 - 630 GPSHSSESLREFMRQKAQARRRQALEEKASALRTRELRSRRLQEVYRQQREAVLGRAVPVVSRTTPGIVT 631 - 700 FVPSSAQSGGLEASGSLESPVLEWSKVTSGMVLGGQEAPGSFCLCLNRAWNHAETLDPPGMGGPQDGRDA 701 - 770 PVLLSASPSLGSLELQDLTTRYLPRGMCIYLDPKEAEHLGTSSSLHLRHKQAQLQALETTAKVLKQRVDS 771 - 840 ...
When the improved inter-domain routing protocol is deployed, an immediate decrease in the number routing table entries should occur, followed by a significant reduction in the rate growth of routing table size (for default-free routers). ...
Domain combinations containing the KaiA/RbsU domain superfamily in Staphylococcus aureus subsp. aureus N315. Domain architectures illustrate each occurrence of the KaiA/RbsU domain superfamily.
Domain combinations containing the KaiA/RbsU domain superfamily in Staphylococcus aureus RF122. Domain architectures illustrate each occurrence of the KaiA/RbsU domain superfamily.
Solution NMR structures provide first structural coverage of the large protein domain family PF08369 and complementary structural coverage of dark
Homer protein homolog 1 or Homer1 is a neuronal protein that in humans is encoded by the HOMER1 gene. Other names are Vesl and PSD-Zip45. Homer1 protein has an N-terminal EVH1 domain, involved in protein interaction, and a C-terminal coiled-coil domain involved in self association. It consists of two major splice variants, short-form (Homer1a) and long-form (Homer1b and c). Homer1a has only EVH1 domain and is monomeric while Homer1b and 1c have both EVH1 and coiled-coil domains and are tetrameric. The coiled-coil can be further separated into N-terminal half and C-terminal half. The N-terminal half of the coiled-coil domain is predicted to be a parallel dimer while the C-terminus half is a hybrid of dimeric and anti-parallel tetrameric coiled-coil. As a whole, long Homer is predicted to have a dumbbell-like structure where two pairs of EVH1 domains are located on two sides of long (~50 nm) coiled-coil domain. Mammals have Homer2 and Homer3, in addition to Homer1, which have similar domain ...
The SCOP classification for the Heat shock protein 70kD (HSP70), peptide-binding 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, taxonomic visualisation and hidden Markov model information.
In the accompanying paper (Nagy, Szláma, Szarka, Trexler, Bányai, Patthy, Reassessing Domain Architecture Evolution of Metazoan Proteins: Major Impact of Gene Prediction Errors) we showed that in the case of UniProtKB/TrEMBL, RefSeq, EnsEMBL and NCBIs GNOMON predicted protein sequences of Metazoan species the contribution of erroneous (incomplete, abnormal, mispredicted) sequences to domain architecture (DA) differences of orthologous proteins might be greater than those of true gene rearrangements. Based on these findings, we suggest that earlier genome-scale studies based on comparison of predicted (frequently mispredicted) protein sequences may have led to some erroneous conclusions about the evolution of novel domain architectures of multidomain proteins. In this manuscript we examine the impact of confusing paralogous and epaktologous multidomain proteins (i.e., those that are related only through the independent acquisition of the same domain types) on conclusions drawn about DA evolution of
Monotopic proteins represent a specialized group of membrane proteins in that they are engaged in biochemical events taking place at the membrane interface. In particular, the monotopic lipid-synthesizing enzymes are able to synthesize amphiphilic lipid products by catalyzing two biochemically distinct molecules (substrates) at the membrane interface. Thus, from an evolutionary point of view, anchoring into the membrane interface enables monotopic enzymes to confer sensitivity to a changing environment by regulating their activities in the lipid biosynthetic pathways in order to maintain a certain membrane homeostasis. We are focused on a plant lipid-synthesizing enzyme DGD2 involved in phosphate shortage stress, and analyzed the potentially important lipid anchoring segments of it, by a set of biochemical and biophysical approaches. A mechanism was proposed to explain how DGD2 adjusts its activity to maintain a proper membrane. In addition, a multivariate-based bioinformatics approach was used ...
Ras is a small GTPase, controlling signal transduction pathways and promoting cell proliferation and survival. KRAS is frequently mutated in cancer. Ras consists of highly homologous catalytic domains and flexible C-terminal hypervariable regions (HVRs) that differ significantly across Ras isoforms. Recent NMR and MD simulations discovered that the HVR of K-Ras4B-GDP extensively interacts with the catalytic domain. However, it weakly interacts with the catalytic domain in the GTP-bound state. Here, using MD simulations we modeled K-Ras4B membrane interaction and dimerization. On the membrane, the catalytic domain takes on multiple orientations, including perpendicular and parallel alignments of the allosteric helices with respect to the membrane normal. In the autoinhibited state, the HVR is sandwiched between the effector lobe and the membrane; in the active state, with the farnesyl anchored into the membrane and the HVR unrestrained, the catalytic domain fluctuates reinlessly, exposing its ...
The SCOP classification for the Zn2/Cys6 DNA-binding 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, taxonomic visualisation and hidden Markov model information.
An R object that contains domain superfamily information for Rat Entrez Genes. This data is prepared based on SUPERFAMILY database, which provides SCOP domain architecture assignments to all completely sequenced genomes including eukaryotic genomes. The domain architecture for an Entrez gene is the protein product with the longest length of amino acids. Thus, domain superfamily information for Rat Entrez gene is a list of domain superfamilies (excluding unknown gap) appearing in its domain architecture.. ...
Journal Article: Structures of the Sgt2/SGTA Dimerization Domain with the Get5/UBL4A UBL Domain Reveal an Interaction that Forms a Conserved Dynamic Interface ...
definition of ILKBP, what does ILKBP mean?, meaning of ILKBP, Integrin-Linked Kinase-Binding Protein, ILKBP stands for Integrin-Linked Kinase-Binding Protein
Complete information for SVEP1 gene (Protein Coding), Sushi, Von Willebrand Factor Type A, EGF And Pentraxin Domain Containing 1, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Domain modeling is an important activity in the early stages of software projects to achieve a common understanding of the problem area among project participants. Domain models describe concepts and...
... , Authors: Dessen P. Published in: Atlas Genet Cytogenet Oncol Haematol.
Hi guys, What are the routine methods by which you generate terminal truncations of a protein of interest for subsequent screening for purification, stability and efficient folding for the purposes of crystallization? My protein has 2 known domains and a conserved C-terminal part which is defined as domain by sequence homology with other proteins. We would like to generate different lengths of the protein containing this C-terminus and screen them for expression, solubility, purification, and folding and thus increase our chances for success. appreciate all help Iva ...
This is probably amateurish and obvious but I was surprised. I created a new site but under an existing domain that was already getting pretty good traffic. After only a few days the new site including individual pages came up #1 in Google or Yahoo searching with 2 words. I guess because the pages are crawled regularly. Seems like it might be OK to group new smaller sites under a common domain under some circumstances. Cheaper and less hassles too.
4GOD: Structures of the Sgt2/SGTA Dimerization Domain with the Get5/UBL4A UBL Domain Reveal an Interaction that Forms a Conserved Dynamic Interface.
SMYD1 antibody (SET and MYND domain containing 1) for ICC/IF, IHC-P, WB. Anti-SMYD1 pAb (GTX119484) is tested in Human, Mouse, Rat samples. 100% Ab-Assurance.
View mouse Ubxn10 Chr4:138709837-138737167 with: phenotypes, sequences, polymorphisms, proteins, references, function, expression
Your website should be located at a domain name thats easy to discover, which means you have to opt for an internet address which is easy to remember a new
A scientific resource for the EH protein domain containing information on structure, function, and domain binding during endocytosis and vesicle trafficking.
Some of the hardest parts of working towards the ideal of a theorist, at least for me, are: (1) making sure that I engage with problems that can be made interesting to the new domain I enter and not just me; (2) engaging with these problems in a way and using tools that can be…
Heres what happened. I have a domain with the PDC and multiple BDCs. Someone took a BDC and moved it to a new domain. I had to bring ...
Oh how sweet the sound of other peoples money! Devoid of the real Truth - Patrick Henry knew that following false hope would lead only to further degradation. The further down the path we are headed the more like beasts we will become.
How many ways protein protein interactions are regulated? - posted in Biochemistry: I wonder how many ways protein-protein interactions are regulated. I know a lot of protein protein interactions are modified by phosphorylaton or other modification. Is there other ways that mediate the protein protein interaction? Thanks!
AICD, the C-terminal tail generated from the proteolytic cleavage of the Amyloid Precursor Protein (APP), has been generating interest for its transcriptional modulatory roles. AICD has been hypothesized to have such a function as it is generated by a gamma-secretase-mediated regulated intramembrane proteolysis step, analogous to the generation of Notch intracellular domain (NICD), a well-known transcriptional regulator, from Notch. The AICD/Fe65/Tip60 ternary complex has been proposed as the working transcriptional regulatory complex and some of its target genes have been reported. However, our knowledge of the functions of AICD is still limited due to difficulties in detecting and manipulating the rapidly degraded peptide. Looking at AICD transcription modulation targets from a genome-wide perspective will aid our understanding of the role of AICD tremendously. To this end, AICD chromatin binding sites were investigated from a genome-wide perspective by performing Chromatin Immunoprecipitation ...
9150PRTHomo sapiens 1Val Met Leu Lys Lys Lys Gln Tyr Thr Ser Ile His His Gly Val Val1 5 10 15Glu Val Asp Ala Ala Val Thr Pro Glu Glu Arg His Leu Ser Lys Met 20 25 30Gln Gln Asn Gly Tyr Glu Asn Pro Thr Tyr Lys Phe Phe Glu Gln Met 35 40 45Gln Asn 502134PRTHomo sapiens 2Ala Pro Lys Asn Glu Leu Val Gln Lys Phe Gln Val Tyr Tyr Leu Gly1 5 10 15Asn Val Pro Val Ala Lys Pro Val Gly Val Asp Val Ile Asn Gly Ala 20 25 30Leu Glu Ser Val Leu Ser Ser Ser Ser Arg Glu Gln Trp Thr Pro Ser 35 40 45His Val Ser Val Ala Pro Ala Thr Leu Thr Ile Leu His Gln Gln Thr 50 55 60Glu Ala Val Leu Gly Glu Cys Arg Val Arg Phe Leu Ser Phe Leu Ala65 70 75 80Val Gly Arg Asp Val His Thr Phe Ala Phe Ile Met Ala Ala Gly Pro 85 90 95Ala Ser Phe Cys Cys His Met Phe Trp Cys Glu Pro Asn Ala Ala Ser 100 105 110Leu Ser Glu Ala Val Gln Ala Ala Cys Met Leu Arg Tyr Gln Lys Cys 115 120 125Leu Asp Ala Arg Ser Gln 130325DNAArtificialPrimer APP_C50_F 3gtaccatatg gtgatgctga agaag 25432DNAArtificialPrimer APP_C50_R 4gtacaagctt ctagttctgc atctgctcaa ...
The BAR (Bin/amphiphysin/Rvs) domain is the most conserved feature in amphiphysins from yeast to human and is also found in endophilins and nadrins. We solved the structure of the Drosophila amphiphysin BAR domain. It is a crescent-shaped dimer that binds preferentially to highly curved negatively charged membranes. With its N-terminal amphipathic helix and BAR domain (N-BAR), amphiphysin can drive membrane curvature in vitro and in vivo. The structure is similar to that of arfaptin2, which we find also binds and tubulates membranes. From this, we predict that BAR domains are in many protein families, including sorting nexins, centaurins, and oligophrenins. The universal and minimal BAR domain is a dimerization, membrane-binding, and curvature-sensing module.
Interplay between cellular membranes and their peripheral proteins drives many processes in eukaryotic cells. Proteins of the Bin/Amphiphysin/Rvs (BAR) domain family, in particular, play a role in cellular morphogenesis, for example curving planar membranes into tubular membranes. However, it is still unclear how F-BAR domain proteins act on membranes. Electron microscopy revealed that, …
A recent study showed that the globular tail of Myo4p is not required for the localization of GFP-MS2-tethered particles to the bud and for the inheritance of ER (Bookwalter et al., 2009). This observation suggested that the globular tail might be dispensable for the localization of endogenous ASH1 mRNA and thus also for inhibition of mating type switching in the daughter cell. It further raised the question of whether the globular tail of Myo4p has any function. Here, we used an experimentally refined, globular tail-lacking Myo4p to confirm the previous findings from Bookwalter et al. (2009) (Fig. S1, A-F).. However, when analyzing mother cell-specific expression of the HO endonuclease in cells expressing a globular tail-lacking Myo4p fragment, we found that this process is impaired (Fig. 2, A and B). The subsequent analysis of ASH1 mRNA localization by in situ hybridization and of Myo4p localization by immunofluorescence staining consistently showed that the globular tail is required for full ...
Protein domain superfamilies in CATH-Gene3D have been subclassified into functional families (or FunFams), which are groups of protein sequences and structures with a high probability of sharing the same function(s). Therefore, the functionally important residues in a family are also expected to be highly conserved.. Information on conserved positions in CATH-Gene3D FunFam alignments is shown through the Alignment tab of the FunFam webpages. Conservation scores have been calculated using Scorecons and columns in the alignment are coloured using a rainbow colour scheme, where the highly conserved residues are shown in red through to positions that are not conserved at all, shown in blue. The conservation scores are also mapped onto a representative protein domain structure.. To investigate putative conserved sites for your protein sequence, run a sequence search against the FunFams and click on the FunFam match Alignment page.. ...
Figure 1. Schematic Representations of the Structure of a CESA Protein and a CSC.. (A) Domain structure of a CESA. The intracellular N-terminal domain contains a Zn binding domain and a variable region and is followed by two transmembrane domains. The large cytoplasmic central catalytic domain is divided into the conserved region, which flanks the plant-specific region on both sides, the variable region(s), which includes the class-specific region, and the conserved region(s). The six subsequent transmembrane domains are followed by the cytoplasmic C-terminal domain. CESA1 phosphorylations on various Ser and Thr residues are indicated (source: PhosPhAt 4.0, Zulawski et al., 2013; and references in the text). Several cysteines in the cytoplasmic loop and within the C-terminal domain that are s-acylated in CESA7 (Kumar 2016b) are depicted in pink. C, cellulose chain; CR1, conserved region 1; CR2, conserved region 2; P-CR, plant-specifc region; S, Ser; T, Thr.. (B) A schematic representation of a ...
The process by which fibronectin (FN), a soluble multidomain protein found in tissue fluids, forms insoluble fibrillar networks in the extracellular matrix is poorly understood. Cryptic sites found in FN type III domains have been hypothesized to function as nucleation points, thereby initiating fibrillogenesis. Exposure of these sites could occur upon tension-mediated mechanical rearrangement of type III domains. Here, we present the solution structures of the second type III domain of human FN ((2)FNIII), and that of an interaction complex between the first two type III domains ((1-2)FNIII). The two domains are connected through a long linker, flexible in solution. A weak but specific interdomain interaction maintains (1-2)FNIII in a closed conformation that associates weakly with the FN N-terminal 30 kDa fragment (FN30 kDa). Disruption of the interdomain interaction by amino-acid substitutions dramatically enhances association with FN30 kDa. Truncation analysis of (1-2)FNIII reveals that the
Cancer arises when genetic mutations in a cell cause abnormal growth that leads to a tumour.. Some cancer drugs exploit this to attack tumour cells by targeting proteins that are mutated from their usual form because of mutations in the genes that encode them.. However, only a fraction of all the mutations that contribute significantly to cancer have been identified.. Thomas Peterson, at the University of Maryland, and colleagues developed a new statistical analysis approach that uses genetic data from cancer patients to find cancer-causing mutations.. Unlike previous studies that focused on mutations in individual genes, the new approach addresses similar mutations shared by families of related proteins.. Specifically, the new method focuses on mutations in sub-components of proteins known as protein domains.. Even though different genes encode them, different proteins can share common protein domains.. The new strategy draws on existing knowledge of protein domain structure and function to ...
The M2 protein of the influenza A virus is a homotetrameric transmembrane proton channel implicated in several stages of the viral replication process. Each of its 97-residue monomers is known to include a transmembrane α-helix. but the structures of the N- and C-terminal domains have not yet been solved. A significant barrier to an atomic level understanding of the M2 protein is the difficulty associated with expression and purification of the full-length protein, which has primarily been studied in the form of truncated constructs covering the amphipathic helix and a short C-terminal segment. This C-terminal segment, which includes residues 46-62, has been shown for a truncated version of the protein to consist of an amphipathic helix lying on the membrane surface. Here, we present SDSL-EPR structural studies using full-length M2 constructs to examine sites 50-54 in the proposed amphipathic helix region of M2. Using power saturation data for the protein reconstituted into vesicles and CW ...
Autotransporter of N-terminal protease passenger domain that cleaves surface-localized virulence factors. The 3-d structure is known (Oomen et al., 2004). The crystal structure of the NalP translocator domain revealed a 12 β-stranded transmembrane beta-barrel containing a central alpha-helix. The transmembrane beta-barrel is stable even in the absence of the alpha-helix. Removal of the helix results in an influx of water into the pore region, suggesting the helix acts as a plug (Khalid and Sansom 2006). The dimensions of the pore fluctuate, but the NalP monomer is sufficient for the transport of the passenger domain in an unfolded or extended conformation (Khalid and Sansom 2006). NalP is subject to phase variation (Oldfield et al. 2013). ...
Autotransporter of N-terminal protease passenger domain that cleaves surface-localized virulence factors. The 3-d structure is known (Oomen et al., 2004). The crystal structure of the NalP translocator domain revealed a 12 β-stranded transmembrane beta-barrel containing a central alpha-helix. The transmembrane beta-barrel is stable even in the absence of the alpha-helix. Removal of the helix results in an influx of water into the pore region, suggesting the helix acts as a plug (Khalid and Sansom 2006). The dimensions of the pore fluctuate, but the NalP monomer is sufficient for the transport of the passenger domain in an unfolded or extended conformation (Khalid and Sansom 2006). NalP is subject to phase variation (Oldfield et al. 2013). ...
When DArcy Wentworth Thompsons On Growth and Form was published 100 years ago, it raised the question of how biological forms arise during development and across evolution. In light of the advances in molecular and cellular biology since then, a succinct modern view of the question states: how do genes encode geometry? Our new special issue is packed with articles that use mathematical and physical approaches to gain insights into cell and tissue patterning, morphogenesis and dynamics, and that provide a physical framework to capture these processes operating across scales.. Read the Editorial by guest editors Thomas Lecuit and L. Mahadevan, as they provide a perspective on the influence of DArcy Thompsons work and an overview of the articles in this issue.. ...
Looking for online definition of AT-rich interactive domain-containing protein 3C in the Medical Dictionary? AT-rich interactive domain-containing protein 3C explanation free. What is AT-rich interactive domain-containing protein 3C? Meaning of AT-rich interactive domain-containing protein 3C medical term. What does AT-rich interactive domain-containing protein 3C mean?
Looking for online definition of G patch domain-containing protein 7 in the Medical Dictionary? G patch domain-containing protein 7 explanation free. What is G patch domain-containing protein 7? Meaning of G patch domain-containing protein 7 medical term. What does G patch domain-containing protein 7 mean?
Hinge region predictor (H-Predictor) predicts putative hinge regions involved in protein oligomerization via the domain-swapping mechanism. Domain swapping is an important mechanism for protein oligomerization, in which a fragment of a protein exchanges with a corresponding fragment of another like protein. The segment of polypeptide chain that links the swapped domain and the main protein is the hinge region. In most experimentally observed domain-swapped oligomers, the swapped domains correspond to one or several secondary structural elements from either the N- or C-termini. Only in some rare instances the swapped domains are positioned in the middle of the protein. The domain-swapped oligomeric structures are, therefore, mainly determined by the location and the properties of the hinge region.. Using a simple contact-based potential for enthalpy and graph theory- based estimation for entropy, H-Predictor quantifies for each residue the propensity as the hinge region. Physically, the ...
Many large coiled-coil proteins are being found associated peripherally with the cytoplasmic face of the organelles of the secretory pathway. Various roles have been proposed for these proteins, including the docking of donor vesicles or organelles to an acceptor organelle prior to fusion, and, in the case of the Golgi apparatus, the stacking of the cisternae [1] [2] [3] [4] [5]. Such critical roles require accurate recruitment to the correct organelle. For the endosomal coiled-coil protein EEA1, targeting requires a carboxy-terminal FYVE domain, which interacts with Rab5 and phosphatidylinositol 3-phosphate (PI(3)P), whereas the Golgi protein GM130 interacts with Golgi membranes via the protein GRASP65 [3] [6] [7]. In this paper, we show that two other mammalian Golgi coiled-coil proteins, golgin-245/p230 and golgin-97, have a conserved domain of about 50 amino acids at their carboxyl termini. This GRIP domain is also found at the carboxyl terminus of several other large coiled-coiled ...
Gain a comprehensive view of secondary and tertiary protein structures in a biopharmaceutical formulation with SGS. Find out more.
Gain a comprehensive view of secondary and tertiary protein structures in a biopharmaceutical formulation with SGS. Find out more.
In this work the affinity maturation of the murine anti c-myc-peptide antibody 9E10 was analysed. Therefore Fab fragments with reversed mutations directed towards germline genes were genetically produced and characterised for their binding to the human c-myc peptide. The epitope recognized by 9E10 consists of the amino acid sequence EQKLISEEDLLRKR of which the key positions LISEXXL are very selectively recognized. The maturation of 9E10 leads to a 3300-fold higher affinity, which is achieved by a faster association as well as by a slower dissociation of the complex. For the gain in affinity formation of additional contacts to the peptide is less important than conformational and/or flexibility changes of the CDRs which are involved in binding. The exceptionally long CDR-H3 contributes essentially to the affinity maturation. The variable light domain serves thereby with its long CDR-L1 and -L3 as a binding platform for the flexible CDR-H3. Changes in specificity of 9E10 are primarily due to ...
4F2hc is a type-II glycoprotein that form covalently-bound heterodimers with several described light chains and whose main function is the transport of amino acids. Likewise, the heavy chain interacts with β-integrins mediating integrin-dependent events such as survival, proliferation, migration and even transformation. Its large C-terminal domain resembles α-amylases structure, but lacking catalytic residues and thus enzymatic activity. In fact, this ectodomain contains the N-terminal domain A, a TIM barrel, connected by 6 residues in α-helix to the C-terminal domain C, comprised of a β-sandwich. Spectroscopic/structural characterization of recombinant 4F2hc-ED shows that its structure in solution is quite similar to that of the crystal, being compact and thermally stable. Moreover, this ectodomain is unable to homodimerize by itself, remaining monomeric in solution. According to the data obtained, the folding/unfolding mechanism of 4F2hc-ED may occur following a 4-state model with 2 ...
2LOU: Structural features of the apelin receptor N-terminal tail and first transmembrane segment implicated in ligand binding and receptor trafficking.
MMLs stimulate WhNV 480-44-4 protein A self-interaction by selling the homotypic and heterotypic interactions of protein A. (A) MBP-tagged protein A fragments
It has been suggested [4] that these transport proteins have evolved from the duplication of an ancestral protein with six transmembrane regions, this hypothesis is based on the conservation of two G-R-[KR] motifs. The first one is located between the second and third transmembrane domains and the second one between transmembrane domains 8 and 9. We have developed two patterns to detect this family of proteins. The first pattern is based on the G-R-[KR] motif; but because this motif is too short to be specific to this family of proteins, we have derived a pattern from a larger region centered on the second copy of this motif. The second pattern is based on a number of conserved residues which are located at the end of the fourth transmembrane segment and in the short loop region between the fourth and fifth segments. Last update: April 2006 / Patterns revised. ...
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.
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.
Burman, E; Elfverson, D; Hansbo, P; Larson, MG; Larsson, K; (2019) Cut topology optimization for linear elasticity with coupling to parametric nondesign domain regions. Computer Methods in Applied Mechanics and Engineering , 350 pp. 462-479. 10.1016/j.cma.2019.03.016 ...
... , Q5VRH9, AS13 2728, U-box domain-containing protein 12antibody, rice, Oryza sativa, developmental biology
... , 10012-H02H1 is produced in HEK293 Cells, with high purity. Animal free. Produced in house. Bulk in stock.
Furuya, F., Poitelea, M., Guo, L., Caspari, T. and Carr, A. M. (2004) Chk1 activation requires Rad9 S/TQ-site phosphorylation to promote association with C-terminal BRCT domains of Rad4TOPBP1. Genes and Development, 18. pp. 1154-1164. ISSN 0890-9369 Full text not available from this repository ...
If you have the timestamp of one of the changed files, then that gives you an exact minute to look at in the access logs, so you just need to look for activity during that minute. You also need to find out if they are only changing files that are writable by the webserver or if they are changing other files as well. If they are changing other files, then its probably being done by FTP, domain control panel or some other server exploit. I just worked on another one of these problems that turned out to be a domain control panel issue ...
Nectin-loved ones molecules have 3 Ig-like domains in their extracellular locations. These 3 Ig-like domains are noted to kind homo- and hetero-dimers with
Histone H2A H2B H3 H4 H2AX Peptides Biotinylated acetylated methylated phosphorylated for use in enzyme assays, histone binding and pulldown experiments
In order to launch a new website what is better for Google? What will be the best solution to be noticed by Google asap? - Use an old domain name already online for 5/7 years (even if the name is not using the keyword you want) - Use a brand new domain name (with the keyword you need inside) Old domain name vs. new domain with a keyword. What is the best solution?
Rubicon (RUN domain protein as Beclin1 interacting and cysteine-rich containing) protein has recently been identified as a novel Beclin1-binding autophagy prote...
multihelical; 3-helical bundle similar to one half of the DEATH domain fold is flanked by two alpha-hairpins forming a four-helical bundle; the axes of the three-helical and four-helical bundles are aproximately orthogonal to each other ...
View mouse Ccdc47 Chr11:106197408-106216344 with: phenotypes, sequences, polymorphisms, proteins, references, function, expression
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Last year we created a new domain and we use Citrix for our external users to be able to run the hosted app. However, there is three use...
eIF4G1兔多克隆抗体(ab80003)可与人样本反应并经ELISA, IHC实验严格验证。中国75%以上现货,所有产品均提供质保服务,可通过电话、电邮或微信获得本地专属技术支持。
The purpose of these volumes is to provide a reference work for the methods of purifying many of the receptors we know about. This be- comes increasingly important as full-length receptors are overexp
PTGIS兔多克隆抗体(ab79846)可与小鼠, 人样本反应并经WB, ELISA实验严格验证,被1篇文献引用。所有产品均提供质保服务,中国75%以上现货。
Планета Королёва - информационный ресурс, посвященный достижениям в области отечественной пилотируемой космонавтики. Социальный информационно-просветительский проект, способствующий развитию научных идей в области космических технологий и расширению масштаба их применения в социально-экономической сфере общества.
Phosphoinositide lipids recruit proteins to the plasma membrane involved in the regulation of cytoskeleton organization and in signalling pathways that control cell polarity and growth. Among those, Rgd1p is a yeast GTPase-activating protein (GAP) specific for Rho3p and Rho4p GTPases, which control actin polymerization and stress signalling pathways. Phosphoinositides not only bind Rgd1p, but also stimulate its GAP activity on the membrane-anchored form of Rho4p. Both F-BAR (F-BAR FCH, and BAR) and RhoGAP domains of Rgd1p are involved in lipid interactions. In the Rgd1p-F-BAR domain, a phosphoinositide-binding site has been recently characterized. We report here the X-ray structure of the Rgd1p-RhoGAP domain, identify by NMR spectroscopy and confirm by docking simulations, a new but cryptic phosphoinositide-binding site, comprising contiguous A1, A1′ and B helices. The addition of helix A1′, unusual among RhoGAP domains, seems to be crucial for lipid interactions. Such a site was totally ...
0025] In certain other embodiments, the VSV vector of the immunogenic composition comprises a G.sub.(ct) mutation and a M.sub.(ncp) mutation. In another embodiment, the G protein encoded by the truncated G gene has a cytoplasmic tail domain consisting of one amino acid (G.sub.(ct-1)) or a cytoplasmic tail domain consisting of nine amino acids (G.sub.(ct-9)). In another embodiment, the M.sub.(ncp) mutation is a mutation of methionine to alanine at position 33 (M33A) and a mutation of methionine to alanine at position 51 (M51A) of the M protein. In one particular embodiment, the immunogenic composition comprises a mutated VSV genome of 3-NPM.sub.(ncp)G.sub.(ct-1)L-5 or 3-NPM.sub.(ncp)G.sub.(ct-9)L-5. In yet other embodiments, the VSV vector of the immunogenic composition further comprises a third class of mutation in its genome, wherein the mutation is a ts mutation, a point mutation, a gene shuffling mutation, a G-stem mutation, an ambisense RNA mutation, a G gene insertion mutation and a ...
... , Authors: Dessen P. Published in: Atlas Genet Cytogenet Oncol Haematol.
Most proteins function by interacting with other molecules. Their interaction interfaces are highly conserved throughout evolution to avoid undesirable interactions that lead to fatal disorders in cells. Rational drug discovery includes computational methods to identify the interaction sites of lead compounds to the target molecules. Identifying and classifying protein interaction interfaces on a large scale can help researchers discover drug targets more efficiently. We introduce a large-scale protein domain interaction interface database called InterPare http://interpare.net . It contains both inter-chain (between chains) interfaces and intra-chain (within chain) interfaces. InterPare uses three methods to detect interfaces: 1) the geometric distance method for checking the distance between atoms that belong to different domains, 2) Accessible Surface Area (ASA), a method for detecting the buried region of a protein that is detached from a
Interactions between GPCRs and their cognate G proteins are known to involve several different domains on both the receptor and the G protein heterotrimer. Within Gα, the best characterized GPCR contact site is the extreme C terminus where residues at positions -3 and -4 are particularly important for specific receptor recognition (Conklin et al., 1993, 1996; Kostenis et al., 1997c; Bahia et al., 1998; Blahos et al., 1998; Liu et al., 2002). We have recently demonstrated the importance of the linker I region of Gαq proteins in constraining the fidelity of receptor recognition. A highly conserved glycine residue in linker I (glycine 66) regulates coupling selectivity indirectly by playing a role in the specificity of nucleotide exchange within Gαq induced by ligand-activated GPCRs (Heydorn et al., 2004). Here, we analyzed 1) the relationship between the linker I region and the extreme C terminus of Gα in determining selective GPCR coupling and 2) whether different GPCRs use different Gα ...
The functional characterization of BAR-domain-containing proteins has expanded quite rapidly over the past few years. Recently, Guerrier and colleagues found that the F-BAR domain of srGAP2 shares the functional properties of I-BAR domain activity (Guerrier et al., 2009), such as those contained in IRSp53 and missing in metastasis (MIM) (Mattila et al., 2007; Millard et al., 2007; Saarikangas et al., 2009) by inducing membrane protrusions, rather than making invaginations as observed with canonical F-BAR proteins (Frost et al., 2007; Itoh et al., 2005). Recent reports (Carlson et al., 2011) and reviews (Heath and Insall, 2008) describing the subclasses of F-BAR-domain-containing proteins categorize srGAP family members into one functionally uniform subgroup; however, our work demonstrates that there are discrete roles and intricate differences between each srGAP family member.. Although the F-BAR domains of the srGAP family are all able to induce filopodia-like membrane protrusions to a greater ...
The non‐conservation in ETS proteins of the hydrophobic residues necessary for stabilization of the putative helix 1 as well as the insertion observed in that region for some ETS proteins, together with our secondary structure prediction, suggest that this region is unlikely to fold as an α‐helix. In the absence of experimental data about the structure adopted by this domain in either a monomeric or oligomeric state, its description as an HLH domain clearly appears to be premature.. The conserved fold of the amino‐terminal domain of ETS proteins is likely to underlie a conserved function. Our results show, however, that the conserved amino‐terminal domains of ETS‐1, ERG‐2 and GABPα are not homotypic oligomerization domains since they failed to replace the conserved amino‐terminal domain of TEL in inducing oligomerization when analyzed in an identical setting (Figure 6). These data are in accordance with other experimental approaches which have led to the conclusion that ETS‐1 ...
Several novel techniques are employed for protein tertiary structure prediction, but the more successful ones are those that rely either solely or partly on template/homology based modeling of full or sub-structures. However, a critical look at the yearly
The tumor suppressor protein, p53, is mutated or dysregulated in nearly all human cancers(1). The amino terminal domains are essential for transcriptional activation in stressed cells and play a vital role in cell cycle regulation, apoptosis and senescence. The transactivation (TAD) and proline rich domains in this region are dynamic and intrinsically disordered; lacking stable secondary or tertiary structure. This region contains multiple binding sites; arguably, the most significant of these is for p53s negative regulator, the E3 ligase, MDM2. An important, but less understood interaction involving the single stranded DNA binding protein, RPA70A, is hypothesized to be involved in maintaining genome integrity(2-4). Additionally, the amino terminus contains an important single nucleotide polymorphism that has demonstrated different affinity for MDM2 and is of significant biological importance in the induction of apoptosis (5). Isothermal titration calorimetry (ITC) and nuclear magnetic resonance (NMR)
DynDom is a program that determines protein domains, hinge axes and amino acid residues involved in the hinge bending. It is fully automated.. You can use DynDom if you have two conformations of the same protein. These may be two X-ray structures, or structures generated using simulation techniques such as molecular dynamics or normal mode analysis.. The application of DynDom provides a view of the conformational change that is easily understood. The conformational change may be quite complicated in detail, but by using DynDom you can visualize it as involving the movement of domains as quasi-rigid bodies. The analysis of a conformational change in terms of domain movements only makes sense if the interdomain deformation is at least comparable to the intradomain deformation. You can use DynDom to assess this, but the results could be misleading if this is not the case.. DynDom allows you to visualize the domain motion in terms of the rotation of one domain relative to another. Here we see the ...