Phosphate-Binding Proteins
Binding Sites
Pyridoxal Phosphate
Fructosephosphates
Molecular Sequence Data
Glucose-6-Phosphate
Amino Acid Sequence
Distribution of binding sequences for the mitochondrial import receptors Tom20, Tom22, and Tom70 in a presequence-carrying preprotein and a non-cleavable preprotein. (1/143)
Preproteins destined for mitochondria either are synthesized with amino-terminal signal sequences, termed presequences, or possess internal targeting information within the protein. The preprotein translocase of the outer mitochondrial membrane (designated Tom) contains specific import receptors. The cytosolic domains of three import receptors, Tom20, Tom22, and Tom70, have been shown to interact with preproteins. Little is known about the internal targeting information in preproteins and the distribution of binding sequences for the three import receptors. We have studied the binding of the purified cytosolic domains of Tom20, Tom22, and Tom70 to cellulose-bound peptide scans derived from a presequence-carrying cleavable preprotein, cytochrome c oxidase subunit IV, and a non-cleavable preprotein with internal targeting information, the phosphate carrier. All three receptor domains are able to bind efficiently to linear 13-mer peptides, yet with different specificity. Tom20 preferentially binds to presequence segments of subunit IV. Tom22 binds to segments corresponding to the carboxyl-terminal part of the presequence and the amino-terminal part of the mature protein. Tom70 does not bind efficiently to any region of subunit IV. In contrast, Tom70 and Tom20 bind to multiple segments within the phosphate carrier, yet the amino-terminal region is excluded. Both charged and uncharged peptides derived from the phosphate carrier show specific binding properties for Tom70 and Tom20, indicating that charge is not a critical determinant of internal targeting sequences. This feature contrasts with the crucial role of positively charged amino acids in presequences. Our results demonstrate that linear peptide segments of preproteins can serve as binding sites for all three receptors with differential specificity and imply different mechanisms for translocation of cleavable and non-cleavable preproteins. (+info)Pht2;1 encodes a low-affinity phosphate transporter from Arabidopsis. (2/143)
An Arabidopsis genomic sequence was recently shown to share similarity with bacterial and eukaryotic phosphate (Pi) transporters. We have cloned the corresponding cDNA, which we named Pht2;1, and subsequently performed gene expression studies and functional analysis of the protein product. The cDNA encodes a 61-kD protein with a putative topology of 12 transmembrane (TM) domains interrupted by a large hydrophilic loop between TM8 and TM9. Two boxes of eight and nine amino acids, located in the N- and C-terminal domains, respectively, are highly conserved among species across all kingdoms (eubacteria, archea, fungi, plants, and animals). The Pht2;1 gene is predominantly expressed in green tissue, the amount of transcript staying constant in leaves irrespective of the Pi status of the shoot; in roots, however, there is a marginal increase in mRNA amounts in response to Pi deprivation. Although the protein is highly similar to eukaryotic sodium-dependent Pi transporters, functional analysis of the Pht2;1 protein in mutant yeast cells indicates that it is a proton/Pi symporter dependent on the electrochemical gradient across the plasma membrane. Its fairly high apparent K(m) for Pi (0.4 mM) and high mRNA content in the shoot, especially in leaves, suggest a role for shoot organs in Pi loading. Pht2;1 thus differs from members of the recently described plant Pi transporter family in primary structure, affinity for Pi, and presumed function. (+info)Faropenem transport across the renal epithelial luminal membrane via inorganic phosphate transporter Npt1. (3/143)
We previously showed that the mouse inorganic phosphate transporter Npt1 operates in the hepatic sinusoidal membrane transport of anionic drugs such as benzylpenicillin and mevalonic acid. In the present study, the mechanism of renal secretion of penem antibiotics was examined by using a Xenopus oocyte expression system. Faropenem (an oral penem antibiotic) was transported via Npt1 with a Michaelis-Menten constant of 0.77 +/- 0.34 mM in a sodium-independent but chloride ion-sensitive manner. When the concentration of chloride ions was increased, the transport activity of faropenem by Npt1 was decreased. Since the concentration gradient of chloride ions is in the lumen-to-intracellular direction, faropenem is expected to be transported from inside proximal tubular cells to the lumen. So, we tested the release of faropenem from Xenopus oocytes. The rate of efflux of faropenem from Npt1-expressing oocytes was about 9.5 times faster than that from control water-injected Xenopus oocytes. Faropenem transport by Npt1 was significantly inhibited by beta-lactam antibiotics such as benzylpenicillin, ampicillin, cephalexin, and cefazolin to 24.9, 40. 5, 54.4, and 26.2% of that for the control, respectively. Zwitterionic beta-lactam antibiotics showed lesser inhibitory effects on faropenem uptake than anionic derivatives, indicating that Npt1 preferentially transports anionic compounds. Other anionic compounds, such as indomethacin and furosemide, and the anion transport inhibitor 4,4'-diisothiocyanostilbene-2,2'-disulfonic acid significantly inhibited faropenem uptake mediated by Npt1. In conclusion, our results suggest that Npt1 participates in the renal secretion of penem antibiotics. (+info)Molecular mechanisms of phosphate and sulphate transport in plants. (4/143)
The application of molecular techniques in recent years has advanced our understanding of phosphate and sulphate transport processes in plants. Genes encoding phosphate and sulphate transporters have been isolated from a number of plant species. The transporters encoded by these genes are related to the major facilitator superfamily of proteins. They are predicted to contain 12 membrane-spanning domains and function as H(+)/H(2)PO(-4) or H(+)/SO(2/-4) cotransporters. Both high-affinity and low-affinity types have been identified. Most research has concentrated on genes that encode transporters expressed in roots. The expression of many of these genes is transcriptionally regulated by signals that respond to the nutrient status of the plant. Nutrient demand and the availability of precursors needed in the assimilatory pathways also regulate transcription of some of these genes. Information on the cell types in which phosphate and sulphate transporters are expressed is becoming available. These data, together with functional characterisation of the transporters, are enabling the roles of various transporters in the overall phosphate and sulphate nutrition of plants to be defined. (+info)Solute pores, ion channels, and metabolite transporters in the outer and inner envelope membranes of higher plant plastids. (5/143)
All plant cells contain plastids. Various reactions are located exclusively within these unique organelles, requiring the controlled exchange of a wide range of solutes, ions, and metabolites. In recent years, several proteins involved in import and/or export of these compounds have been characterized using biochemical and electrophysiological approaches, and in addition have been identified at the molecular level. Several solute channels have been identified in the outer envelope membrane. These porin-like proteins in the outer envelope membrane were formerly thought to be quite unspecific, but have now been shown to exhibit significant substrate specificity and to be highly regulated. Therefore, the inter-envelope membrane space is not as freely accessible as previously thought. Transport proteins in the inner envelope membrane have been characterized in more detail. It has been proved unequivocally that a family of proteins (including triose phosphate-/phosphoenolpyruvate-, and glucose 6-phosphate-specific transporters) permit the exchange of inorganic phosphate and phosphorylated intermediates. A new type of plastidic 2-oxoglutarate/malate transporter has been identified and represents the first carrier with 12 putative transmembrane domains, to be located in the inner envelope membrane. The plastidic ATP/ADP transporter also contains 12 putative transmembrane domains and possesses striking structural similarity to ATP/ADP transporters found in intracellular, human pathogenic bacteria. (+info)Mutations of the caenorhabditis elegans brain-specific inorganic phosphate transporter eat-4 affect habituation of the tap-withdrawal response without affecting the response itself. (6/143)
The studies reported here were designed to investigate the role of the mutation eat-4 in the response to tap and in habituation in the nematode Caenorhabditis elegans. In C. elegans eat-4 has been found to affect a number of glutamatergic pathways. It has been hypothesized to positively regulate glutaminase activity and therefore glutamatergic neurotransmission. In the eat-4(ky5) loss-of-function worms, there is presumably insufficient glutamate available for sustained transmission. In the experiments reported here eat-4 worms showed no differences from wild-type in the magnitude of response to a single tap, indicating that the neural circuit underlying the response was intact and functional in the mutant worms. However, when eat-4 worms were given repeated taps the resulting habituation was different from that seen in wild-type worms: eat-4 worms habituate more rapidly and recover more slowly than wild-type worms at all interstimulus intervals tested. In addition, eat-4 worms do not show dishabituation. The same transgene rescues pharyngeal activity defects and both the habituation and dishabituation deficits seen in the eat-4 worms. Our results suggest that neurotransmitter regulation plays a role in habituation and may play a role in dishabituation. (+info)Regulation of cation-coupled high-affinity phosphate uptake in the yeast Saccharomyces cerevisiae. (7/143)
Studies of the high-affinity phosphate transporters in the yeast Saccharomyces cerevisiae using mutant strains lacking either the Pho84 or the Pho89 permease revealed that the transporters are differentially regulated. Although both genes are induced by phosphate starvation, activation of the Pho89 transporter precedes that of the Pho84 transporter early in the growth phase in a way which may possibly reflect a fine tuning of the phosphate uptake process relative to the availability of external phosphate. (+info)Zinc deficiency up-regulates expression of high-affinity phosphate transporter genes in both phosphate-sufficient and -deficient barley roots. (8/143)
Phosphate (P) is taken up by plants through high-affinity P transporter proteins embedded in the plasma membrane of certain cell types in plant roots. Expression of the genes that encode these transporters responds to the P status of the plants, and their transcription is normally tightly controlled. However, this tight control of P uptake is lost under Zn deficiency, leading to very high accumulation of P in plants. We examined the effect of plant Zn status on the expression of the genes encoding the HVPT1 and HVPT2 high-affinity P transporters in barley (Hordeum vulgare L. cv Weeah) roots. The results show that the expression of these genes is intimately linked to the Zn status of the plants. Zn deficiency induced the expression of genes encoding these P transporters in plants grown in either P-sufficient or -deficient conditions. Moreover, the role of Zn in the regulation of these genes is specific in that it cannot be replaced by manganese (a divalent cation similar to Zn). It appears that Zn plays a specific role in the signal transduction pathway responsible for the regulation of genes encoding high-affinity P transporters in plant roots. The significance of Zn involvement in the regulation of genes involved in P uptake is discussed. (+info)Phosphate-binding proteins are a type of protein that play a crucial role in regulating the concentration of phosphates in cells. They function by binding to phosphate ions and facilitating their transport, storage, or excretion. These proteins can be found in various organisms, including bacteria, plants, and animals.
In humans, one example of a phosphate-binding protein is the plasma protein known as fetuin-A. Fetuin-A helps regulate the amount of phosphate in the blood by binding to it and preventing it from forming insoluble precipitates with calcium, which can lead to the formation of kidney stones or calcifications in soft tissues.
Another example is the intracellular protein called alkaline phosphatase, which plays a role in removing phosphate groups from molecules within the cell. This enzyme helps regulate the levels of phosphates and other ions within the cell, as well as contributing to various metabolic processes.
Overall, phosphate-binding proteins are essential for maintaining proper phosphate homeostasis in the body, which is critical for numerous physiological functions, including energy metabolism, bone health, and signal transduction.
Phosphates, in a medical context, refer to the salts or esters of phosphoric acid. Phosphates play crucial roles in various biological processes within the human body. They are essential components of bones and teeth, where they combine with calcium to form hydroxyapatite crystals. Phosphates also participate in energy transfer reactions as phosphate groups attached to adenosine diphosphate (ADP) and adenosine triphosphate (ATP). Additionally, they contribute to buffer systems that help maintain normal pH levels in the body.
Abnormal levels of phosphates in the blood can indicate certain medical conditions. High phosphate levels (hyperphosphatemia) may be associated with kidney dysfunction, hyperparathyroidism, or excessive intake of phosphate-containing products. Low phosphate levels (hypophosphatemia) might result from malnutrition, vitamin D deficiency, or certain diseases affecting the small intestine or kidneys. Both hypophosphatemia and hyperphosphatemia can have significant impacts on various organ systems and may require medical intervention.
In the context of medical and biological sciences, a "binding site" refers to a specific location on a protein, molecule, or cell where another molecule can attach or bind. This binding interaction can lead to various functional changes in the original protein or molecule. The other molecule that binds to the binding site is often referred to as a ligand, which can be a small molecule, ion, or even another protein.
The binding between a ligand and its target binding site can be specific and selective, meaning that only certain ligands can bind to particular binding sites with high affinity. This specificity plays a crucial role in various biological processes, such as signal transduction, enzyme catalysis, or drug action.
In the case of drug development, understanding the location and properties of binding sites on target proteins is essential for designing drugs that can selectively bind to these sites and modulate protein function. This knowledge can help create more effective and safer therapeutic options for various diseases.
Pyridoxal phosphate (PLP) is the active form of vitamin B6 and functions as a cofactor in various enzymatic reactions in the human body. It plays a crucial role in the metabolism of amino acids, carbohydrates, lipids, and neurotransmitters. Pyridoxal phosphate is involved in more than 140 different enzyme-catalyzed reactions, making it one of the most versatile cofactors in human biochemistry.
As a cofactor, pyridoxal phosphate helps enzymes carry out their functions by facilitating chemical transformations in substrates (the molecules on which enzymes act). In particular, PLP is essential for transamination, decarboxylation, racemization, and elimination reactions involving amino acids. These processes are vital for the synthesis and degradation of amino acids, neurotransmitters, hemoglobin, and other crucial molecules in the body.
Pyridoxal phosphate is formed from the conversion of pyridoxal (a form of vitamin B6) by the enzyme pyridoxal kinase, using ATP as a phosphate donor. The human body obtains vitamin B6 through dietary sources such as whole grains, legumes, vegetables, nuts, and animal products like poultry, fish, and pork. It is essential to maintain adequate levels of pyridoxal phosphate for optimal enzymatic function and overall health.
Fructose-1,6-bisphosphate (also known as fructose 1,6-diphosphate or Fru-1,6-BP) is the chemical compound that plays a crucial role in cellular respiration and glucose metabolism. It is not accurate to refer to "fructosephosphates" as a medical term, but fructose-1-phosphate and fructose-1,6-bisphosphate are important fructose phosphates with specific functions in the body.
Fructose-1-phosphate is an intermediate metabolite formed during the breakdown of fructose in the liver, while fructose-1,6-bisphosphate is a key regulator of glycolysis, the process by which glucose is broken down to produce energy in the form of ATP. Fructose-1,6-bisphosphate allosterically regulates the enzyme phosphofructokinase, which is the rate-limiting step in glycolysis, and its levels are tightly controlled to maintain proper glucose metabolism. Dysregulation of fructose metabolism has been implicated in various metabolic disorders, including insulin resistance, type 2 diabetes, and nonalcoholic fatty liver disease (NAFLD).
Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.
Glucose-6-phosphate (G6P) is a vital intermediate compound in the metabolism of glucose, which is a simple sugar that serves as a primary source of energy for living organisms. G6P plays a critical role in both glycolysis and gluconeogenesis pathways, contributing to the regulation of blood glucose levels and energy production within cells.
In biochemistry, glucose-6-phosphate is defined as:
A hexose sugar phosphate ester formed by the phosphorylation of glucose at the 6th carbon atom by ATP in a reaction catalyzed by the enzyme hexokinase or glucokinase. This reaction is the first step in both glycolysis and glucose storage (glycogen synthesis) processes, ensuring that glucose can be effectively utilized for energy production or stored for later use.
G6P serves as a crucial metabolic branch point, leading to various pathways such as:
1. Glycolysis: In the presence of sufficient ATP and NAD+ levels, G6P is further metabolized through glycolysis to generate pyruvate, which enters the citric acid cycle for additional energy production in the form of ATP, NADH, and FADH2.
2. Gluconeogenesis: During periods of low blood glucose levels, G6P can be synthesized back into glucose through the gluconeogenesis pathway, primarily occurring in the liver and kidneys. This process helps maintain stable blood glucose concentrations and provides energy to cells when dietary intake is insufficient.
3. Pentose phosphate pathway (PPP): A portion of G6P can be shunted into the PPP, an alternative metabolic route that generates NADPH, ribose-5-phosphate for nucleotide synthesis, and erythrose-4-phosphate for aromatic amino acid production. The PPP is essential in maintaining redox balance within cells and supporting biosynthetic processes.
Overall, glucose-6-phosphate plays a critical role as a central metabolic intermediate, connecting various pathways to regulate energy homeostasis, redox balance, and biosynthesis in response to cellular demands and environmental cues.
An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.
In the context of medicine and pharmacology, "kinetics" refers to the study of how a drug moves throughout the body, including its absorption, distribution, metabolism, and excretion (often abbreviated as ADME). This field is called "pharmacokinetics."
1. Absorption: This is the process of a drug moving from its site of administration into the bloodstream. Factors such as the route of administration (e.g., oral, intravenous, etc.), formulation, and individual physiological differences can affect absorption.
2. Distribution: Once a drug is in the bloodstream, it gets distributed throughout the body to various tissues and organs. This process is influenced by factors like blood flow, protein binding, and lipid solubility of the drug.
3. Metabolism: Drugs are often chemically modified in the body, typically in the liver, through processes known as metabolism. These changes can lead to the formation of active or inactive metabolites, which may then be further distributed, excreted, or undergo additional metabolic transformations.
4. Excretion: This is the process by which drugs and their metabolites are eliminated from the body, primarily through the kidneys (urine) and the liver (bile).
Understanding the kinetics of a drug is crucial for determining its optimal dosing regimen, potential interactions with other medications or foods, and any necessary adjustments for special populations like pediatric or geriatric patients, or those with impaired renal or hepatic function.
Protein binding, in the context of medical and biological sciences, refers to the interaction between a protein and another molecule (known as the ligand) that results in a stable complex. This process is often reversible and can be influenced by various factors such as pH, temperature, and concentration of the involved molecules.
In clinical chemistry, protein binding is particularly important when it comes to drugs, as many of them bind to proteins (especially albumin) in the bloodstream. The degree of protein binding can affect a drug's distribution, metabolism, and excretion, which in turn influence its therapeutic effectiveness and potential side effects.
Protein-bound drugs may be less available for interaction with their target tissues, as only the unbound or "free" fraction of the drug is active. Therefore, understanding protein binding can help optimize dosing regimens and minimize adverse reactions.
Perilipin-3
Nicotinic acid adenine dinucleotide phosphate
Phosphatidylinositol 3-phosphate
PCYT1A
Neurotoxicity
Osteonectin
Pib2
Phytophthora megakarya
CRYM
Mannose 6-phosphate
ZFYVE1
TPI1
Narayanaswamy Srinivasan
TSTA3
Kinetic exclusion assay
Beryllium fluoride
Walker motifs
Nest (protein structural motif)
Easy Cheese
NTP binding site
Translocase
Estramustine phosphate
Extracellular fluid
Protein phosphatase
S1PR1
Staphylococcus epidermidis
SOS1
Alkaline phosphatase
Cation-dependent mannose-6-phosphate receptor
Glucose-6-phosphate dehydrogenase
RCSB PDB - 7EW7: Cryo-EM structure of SEW2871-bound Sphingosine-1-phosphate receptor 1 in complex with Gi protein
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SMART: Schnipsel domain PH
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WikiGenes
Putative1
- Mouse protein citron, a putative rho/rac effector that binds to the GTP-bound forms of rho and rac. (embl.de)
Ions6
- Proteins that bind to and are involved in the metabolism of phosphate ions. (uams.edu)
- This electrode showed much larger potential change to phosphate than other ions. (ieice.org)
- In response to kinases and phosphatases, these phosphate ions attach and detach from different molecules, forming a constantly shifting pool. (medscape.com)
- It binds to metal ions and may aid in the transport of copper. (sigmaaldrich.com)
- The chromatography medium provides very high binding capacity for histidine-tagged proteins and shows negligible leakage of Ni 2+ ions. (sigmaaldrich.com)
- Calcium then reacts with bound phosphate ions leading to precipitation of calcium phosphate. (medscape.com)
Intracellular8
- or a shift of phosphate from the extracellular to the intracellular space. (medscape.com)
- Most often it is caused by long-term, relatively low phosphate intake in the setting of a sudden increase in intracellular phosphate requirements. (medscape.com)
- Phosphate is a predominantly intracellular anion with a concentration of approximately 100 mmol/L, although determination of the precise intracellular concentration has been difficult. (medscape.com)
- Most intracellular phosphate is either complexed or bound to proteins and lipids. (medscape.com)
- however, because the intracellular concentration of phosphate is greater than the extracellular concentration, phosphate entry into cells requires a facilitated transport process. (medscape.com)
- Several sodium-coupled transport proteins have been identified that enable intracellular uptake of phosphate by taking advantage of the steep extracellular-to-intracellular sodium gradient. (medscape.com)
- These elevated extracellular levels may result in increased intracellular levels, calcium-phosphate nucleation, and crystalline precipitation. (medscape.com)
- 1994). High-res- belongs to the family of intracellular lipid bind- olution crystal structures (Sacchetti ni et al. (lu.se)
Mannose 6-phosph2
- Mannose-6-phosphate receptor binding protein 1 (M6PRBP1) is a protein which in humans is encoded by the M6PRBP1 gene. (wikipedia.org)
- The mannose-6-phosphate receptor-binding properties of TIP47 are disputed, despite the designation of M6PRBP1 as TIP47's gene symbol. (wikipedia.org)
Import ATP-binding1
- Maltose/maltodextrin import ATP-binding protein MalK aka B4035, component of Maltooligosaccharide porter. (lbl.gov)
Glycerol-3-phosphate d3
- Glycerol-3-phosphate dehydrogenase 2 is a novel factor H-, factor H-like protein 1-, and plasminogen-binding surface protein of Candida albicans. (leibniz-hki.de)
- One 52-kDa protein was eluted and identified by mass spectrometry as glycerol-3-phosphate dehydrogenase 2 (Gpd2). (leibniz-hki.de)
- Predicted to be part of glycerol-3-phosphate dehydrogenase complex. (mcw.edu)
Genes2
- TIP47 belongs to the peripilin protein family and shares significant homology with the other genes of this family, including perilipin and adipophilin. (wikipedia.org)
- SIRT1 is localized in the nucleus and can deacetylate numerous proteins such as tumor suppressor protein (p53), Ku70, NF-κB, and forkhead proteins which modulate genes that control cellular stress resistance ( Smith, 2002 ). (frontiersin.org)
Kinases4
- Ser/Thr protein kinases such as the Akt/Rac family, the beta-adrenergic receptor kinases, the mu isoform of PKC and the trypanosomal NrkA family. (embl.de)
- Tyrosine protein kinases belonging to the Btk/Itk/Tec subfamily. (embl.de)
- Screen Quest™ assay kits, a set of HTS-ready tools for high throughput screening of biochemical and cellular targets such as protein kinases, proteases, HDAC, cell apoptosis and cytoxicity, GPCR, ion channels, ADME/metabolism and transporters. (stratech.co.uk)
- it is involved in skeletal muscle contraction, excitation-contraction coupling in cardiac and smooth muscle, and activation of protein kinases and enzyme phosphorylation. (msdmanuals.com)
Receptors5
- Our structural and functional assays demonstrate the different binding modes of chemically distinct agonists of S1PRs, reveal the mechanical switch that activates these receptors, and provide a framework for understanding ligand selectivity and G protein coupling. (rcsb.org)
- Mannose 6-phosphate receptors (MPRs) deliver lysosomal hydrolase from the Golgi to endosomes and then return to the Golgi complex. (wikipedia.org)
- M6PRBP1 has been shown to interact with both Mannose 6-phosphate receptors. (wikipedia.org)
- Agents that affect the function of G-protein coupled SPHINGOSINE 1-PHOSPHATE RECEPTORS. (bvsalud.org)
- Their binding to the receptors blocks lymphocyte migration and are often used as IMMUNOSUPPRESSANTS. (bvsalud.org)
Transport Proteins1
- Saier, M.H., Jr. Molecular phylogeny as a basis for the classification of transport proteins from bacteria, archaea and eukarya. (enzyme-database.org)
High affinity2
- The chelating binding mode accounts for the high affinity of this protein-carbohydrate interaction. (nature.com)
- high-affinity phosphate transporter [Ensembl]. (ntu.edu.sg)
Subunit2
- The antibacterial activity of tedizolid is mediated by binding to the 50S subunit of the bacterial ribosome resulting in inhibition of protein synthesis. (centerwatch.com)
- maltose ABC transporter ATP binding subunit (EC 7.5.2.1). (lbl.gov)
Nucleotide1
- Regulators of small G-proteins like guanine nucleotide releasing factor GNRP (Ras-GRF) (which contains 2 PH domains), guanine nucleotide exchange proteins like vav, dbl, SoS and Saccharomyces cerevisiae CDC24, GTPase activating proteins like rasGAP and BEM2/IPL2, and the human break point cluster protein bcr. (embl.de)
Macromolecules1
- It also has a role in binding of heme groups, macromolecules and phosphate groups in the binding sites of proteins. (sigmaaldrich.com)
Superfamily2
- Separately, the unknown contigs were also translated using all possible open reading frames and subsequently processed with SUPERFAMILY version 1.75 ( 13 ) to identify potential homologies with known proteins. (cdc.gov)
- ABC superfamily ATP binding cassette transporter, ABC. (ntu.edu.sg)
Gene1
- The protein encoded by this gene interacts with the cytoplasmic domains of both cation-independent and cation-dependent MPRs, and is required for endosome-to-Golgi transport. (wikipedia.org)
Lipid3
- TIP47 protein is most commonly described in the scientific literature as a coat protein for lipid droplets. (wikipedia.org)
- The perilipin family of structural lipid droplet proteins: stabilization of lipid droplets and control of lipolysis" (PDF). (wikipedia.org)
- The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. (nih.gov)
Lipids1
- Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids. (embl.de)
Residues2
- and binds plasminogen, via lysine residues. (leibniz-hki.de)
- Two basic residues are key in binding with phosphoinositides: one forms hydrogen bonds with the 3-phosphate of PI(3)P and another forms hydrogen bonds with the 4-and 5-hydroxyl groups of PI(3)P. (nih.gov)
Sequence2
- Based on primary sequence comparisons, β subunits are predicted to be modular structures composed of five domains (A-E) that are related to the large family of membrane-associated guanylate kinase proteins. (jneurosci.org)
- The structural comparison of binding sites is especially useful when applied on distantly related proteins as a comparison solely based on the amino acid sequence is not sufficient in such cases. (uni-marburg.de)
Concentration8
- Linear relationship between membrane potetial and phosphate concentration was observed in the range of 0.2-5OmM. (ieice.org)
- Phosphate concentration is characterized by a high physiologic variation, depending on age, gender, physiologic state (eg, pregnancy), and even season (due to the seasonal variation of vitamin D, which is directly involved in the regulation of phosphate concentration). (medscape.com)
- Phosphate concentration in plasma and serum will increased in unseparated specimens stored at room temperature for longer time. (medscape.com)
- As phosphates concentration is higher inside RBC, hemolysis will lead to increase in phosphates plasma/serum concentration. (medscape.com)
- Phosphate concentration increases by 4-5 mg/dl per day in hemolyzed samples stored at 4°C or RT. (medscape.com)
- Prolonged storage at RT and delay testing/separation lead to hydrolysis of phosphate esters (eg, glucose phosphate, creatinine phosphate) and overestimation of phosphate concentration. (medscape.com)
- To prevent the binding of host cell proteins with exposed histidines, it is essential to include imidazole at a low concentration in the sample and binding buffer ( Optimizing purification of histidine-tagged proteins ). (sigmaaldrich.com)
- The optimal concentration of imidazole needed in the sample and buffer to obtain the best purity and yield differs from protein to protein. (sigmaaldrich.com)
Membrane4
- The membrane potential change was observed selectively to phosphate. (ieice.org)
- Phospholipase D (PLD) catalyzes the hydrolysis of the phosphodiester bond of phosphatidylcholine to generate membrane-bound phosphatidic acid and choline. (nih.gov)
- Each pseudopilin protein caps an XcpG protofilament in an overall pseudopilus compatible with dimensions of the periplasm and the outer membrane-spanning secretin through which substrates pass. (bvsalud.org)
- An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. (enzyme-database.org)
Phosphatidylinositol1
- A majority of PX domain containing proteins binds phosphatidylinositol-3-phosphate (PI3P) at this site. (nih.gov)
Regulation3
- Constam, D. B. & Robertson, E. J. Regulation of bone morphogenetic protein activity by pro domains and proprotein convertases. (nature.com)
- The addition and deletion of phosphate groups to enzymes and proteins are common mechanisms for the regulation of their activity. (medscape.com)
- Several S. cerevisiae proteins involved in cell cycle regulation and bud formation like BEM2, BEM3, BUD4 and the BEM1-binding proteins BOI2 (BEB1) and BOI1 (BOB1). (embl.de)
ATPase1
- phosphate ABC transporter ATPase [Ensembl]. (ntu.edu.sg)
Cytoskeletal1
- Cytoskeletal proteins such as dynamin (see IPR001401 ), Caenorhabditis elegans kinesin-like protein unc-104 (see IPR001752 ), spectrin beta-chain, syntrophin (2 PH domains) and S. cerevisiae nuclear migration protein NUM1. (embl.de)
Calcium7
- Are calcium-based phosphate binders ever preferable in dialysis patients? (uams.edu)
- In addition to serum phosphate studies, serum calcium and magnesium studies can be helpful for identifying underlying causes. (medscape.com)
- Abnormalities of proximal tubular function included reduced reabsorption of beta-2-microglobulin, retinol binding protein, calcium and phosphate. (cdc.gov)
- These calcium salts consist primarily of hydroxyapatite crystals or amorphous calcium phosphate. (medscape.com)
- Ectopic calcification can occur in the setting of hypercalcemia and/or hyperphosphatemia when the calcium-phosphate product exceeds 70 mg 2 /dL 2 , without preceding tissue damage. (medscape.com)
- The remaining 60% includes ionized calcium plus calcium complexed with phosphate and citrate. (msdmanuals.com)
- Total calcium (ie, protein-bound, complexed, and ionized calcium) is usually what is determined by clinical laboratory measurement. (msdmanuals.com)
Receptor3
- The canonical TGFβ signalling pathway involves ligand-dependent assembly of a heteromeric receptor complex, receptor-kinase activation and subsequent phosphorylation and activation of SMAD proteins, which are transcriptional regulators that consequently accumulate in the nucleus. (nature.com)
- Protein binding site comparisons are frequently used receptor-based techniques in early stages of the drug development process. (uni-marburg.de)
- The heavy chain is responsible for both receptor some species of the genus Clostridium, in particular, Clostridium binding via its C-terminal (CT) binding domain [4,5] (HC) and botulinum, C. butyricum, C. baratii, and C. argentinense. (cdc.gov)
Ensembl3
- Phosphate transport ATP-binding protein PstB (TC 3.A.1.7.1) [Ensembl]. (ntu.edu.sg)
- phosphate transporter ATP-binding protein [Ensembl]. (ntu.edu.sg)
- PstB protein [Ensembl]. (ntu.edu.sg)
Genome1
- GapMind relies on the predicted proteins in the genome and does not search the six-frame translation. (lbl.gov)
Structural5
- SCOP: Structural Classification of Proteins and ASTRAL. (berkeley.edu)
- SCOPe: Structural Classification of Proteins - extended. (berkeley.edu)
- Figure 5: Structural comparison of α-DG-binding LG domains. (nature.com)
- Matching of structural motifs using hashing on residue labels and geometric filtering for protein function prediction. (uni-marburg.de)
- Moreover, the structure raises interesting possibilities about how type 2 secretion-system substrates may interact with the secretion machinery and demonstrates the utility of new artificial intelligence protein structure-prediction algorithms in making challenging structural targets tractable. (bvsalud.org)
Nucleic2
- Phosphate is an integral component of the nucleic acids that comprise DNA and RNA. (medscape.com)
- iFluor™ superior fluorescent labelling dyes, optimised for labelling proteins and nucleic acids. (stratech.co.uk)
Pediatric2
- Burosumab, an IgG1 monoclonal antibody that binds excess fibroblast growth factor 23 (FGF23), is approved for treatment of X-linked hypophosphatemia and of FGF23-related hypophosphatemia in tumor-induced osteomalacia associated with phosphaturic mesenchymal tumors that cannot be curatively resected or localized, in adults and pediatric patients aged 2 years or older. (medscape.com)
- Neuropsychiatric events: Patients with influenza, including those receiving oseltamivir phosphate capsules, particularly pediatric patients, may be at an increased risk of confusion or abnormal behavior early in their illness. (nih.gov)
Serum4
- Hypophosphatemia is defined as a serum phosphate level of less than 2.5 mg/dL (0.8 mmol/L) in adults. (medscape.com)
- A well-accepted theory for renal toxicity is the release of uranium from serum bicarbonate complex in the kidney that allows uranium to bind to available phosphate and protein. (cdc.gov)
- When rapid elevations of serum phosphate levels are documented, the most urgent associated problem is typically hypocalcemia with tetany, seizures, and hypotension. (medscape.com)
- The most common assay for phosphate determination in clinical laboratories is based on a spectrophotometric method of complexing the serum inorganic phosphate with ammonium molibdate at low pH and formation of an absorbent phosphomolibdate complex that is measured by the spectrophotometer instrument. (medscape.com)
Molecules3
- A single glucuronic acid-β1,3-xylose disaccharide repeat straddles a Ca 2+ ion in the LG4 domain, with oxygen atoms from both sugars replacing Ca 2+ -bound water molecules. (nature.com)
- These programs are utilized to screen entire libraries of molecules for a possible ligand of a binding site and to furthermore estimate in which conformation the ligand will most likely bind. (uni-marburg.de)
- [ 1 , 2 ] PEG, a water-soluble linear polymer, appears to accelerate antibody-RBC binding by steric exclusion of water molecules in the diluents and to promote antibody detection. (medscape.com)
Heterotrimeric1
- Herein, we present five cryo-electron microscopy structures of S1PRs bound to diverse drug agonists and the heterotrimeric Gi protein. (rcsb.org)
Elucidate2
- These models are being used to systematically elucidate proteins required for cutaneous carcinogenesis and to test their potential role as therapeutic targets. (stanford.edu)
- Transcription factor binding motifs help to elucidate regulatory mechanism. (systemsbiology.net)
Differentiation1
- IFABP and the binding thermodynamics (Richieri growth and differentiation (Glatz & van der et al. (lu.se)
Sodium2
- 20 mM sodium phosphate, 0.5 M NaCl, 20 to 40 mM imidazole, pH 7.4. (sigmaaldrich.com)
- Each 1 millilitre (mL) of solution for injection contains 3.32 mg of dexamethasone (as dexamethasone sodium phosphate) which is equivalent to 4.00 mg of dexamethasone phosphate or 4.37 mg dexamethasone sodium phosphate. (who.int)
Interactions1
- Through these interactions, PH domains play a role in recruiting proteins to different membranes, thus targeting them to appropriate cellular compartments or enabling them to interact with other components of the signal transduction pathways. (embl.de)
Membranes2
- The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction. (nih.gov)
- a sensitive and robust tool for detection of proteins in solutions and solid surfaces (such as gels and membranes). (stratech.co.uk)
Homeostasis1
- In view of the sheer breadth of influence of this mineral, the fact that phosphate homeostasis is a highly regulated process is not surprising. (medscape.com)
Bone3
- The bulk of total body phosphate resides in bone as part of the mineralized extracellular matrix. (medscape.com)
- Approximately 300 mg of phosphate per day enters and exits bone tissue. (medscape.com)
- Excessive losses or failure to add phosphate to bone leads to osteomalacia. (medscape.com)
TIGRFam1
- Candidates for each step are identified by using ublast (a fast alternative to protein BLAST) against a database of manually-curated proteins (most of which are experimentally characterized) or by using HMMer with enzyme models (usually from TIGRFam ). (lbl.gov)