• Two arginines in this domain are responsible for hydrogen bonding phosphotyrosine residues on an Ac-LYASSNPApY-NH2 peptide in the juxtamembrane region of the insulin receptor. (wikipedia.org)
  • The SH2 domain binds to phosphotyrosine residues in RTKs such as PDGF and EGF, non-RTKs such as Bcr/Abl and FAK, and docking proteins such as FRS-2 and Gab1. (rndsystems.com)
  • The phosphorylation of proteins at tyrosine residues is critical in the growth signaling induced by Epo. (drugbank.com)
  • There are no totally invariant residues within the PH domain. (embl.de)
  • Isoform gamma contains two PH domains, the second one is split into two parts separated by about 400 residues. (embl.de)
  • Different families of SH2 domains may have different binding specificity, which is usually determined by a few residues C-terminal with respect to the pY (positions +1 to +4). (eu.org)
  • The residue at pY+2 does not make direct side chain interactions with the SH2 domain, but aromatic residues are not allowed. (eu.org)
  • Positively charged residues are disfavoured at pY-1 and pY-2 due to the positively charged SH2 domain surface, but are tolerated when pY+1 and pY+3 are strong residues. (eu.org)
  • This domain was initially shown to binds peptides with a NPXY motif with differing requirements for phosphorylation of the tyrosine, although more recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. (umbc.edu)
  • In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. (umbc.edu)
  • [8] Mutagenesis studies of type I IFNs, IFNAR1 and IFNAR2 demonstrated important binding residues, i.e. "hotspots", on the type I IFN subtypes which influenced its ability to bind to IFNAR2. (wikidoc.org)
  • PTB area binding specificity is certainly conferred by residues N-terminal towards the phosphotyrosine residue. (researchensemble.com)
  • It had been soon found that many PTB domains bind to tyrosine residues irrespective of their phosphorylation position. (researchensemble.com)
  • 2003 As opposed to PTB domains SH2 domains recognize an important phosphotyrosine and adjacent C-terminal residues. (researchensemble.com)
  • The Src homology 2 (SH2) domains are about 100 residues in length with an average of 28% pairwise residue identity (Pfam code PF00017). (lu.se)
  • SH2 domains mediate intramolecular recognition and intermolecular protein-protein association almost invariably by binding to phosphorylated tyrosine (pY) residues in specific sequence contexts. (lu.se)
  • The bacterial SH2 domains are not only capable of binding proteins or peptides in a Tyr phosphorylation-dependent manner, some bind pTyr itself with micromolar affinities, a property not observed for mammalian SH2 domains. (rcsb.org)
  • In the present study, we examined the role of protein tyrosine phosphorylation and the mitogen-activated protein kinases, ERK1/2,in mediating BK-induced AP-1 and DNA replication in cultured rat mesangial cells. (nih.gov)
  • BK (10(-9) to 10(-7) M) stimulated a rapid increase in tyrosine phosphorylation of multiple proteins with an estimated molecular mass of 120-130, 90-95, and 44-42 kDa. (nih.gov)
  • AP-1 pathway and that BK mitogenic signaling is critically dependent on protein tyrosine phosphorylation. (nih.gov)
  • A. Kashishian, A. Kazlauskas, J.A. Cooper, "Phosphorylation sites in the PDGF receptor with different specificities for binding GAP and PI3 kinase in vivo," The EMBO Journal, 11[4]:1373-82, 1992. (the-scientist.com)
  • Subsequent studies have shown that, while binding of SH2 domains to their target proteins is strictly regulated by tyrosine phosphorylation, most PTB domains actually bind to their (nonphosphorylated) targets constitutively. (chemdiv.com)
  • Tyrosine phosphorylation of GRB2 SH3 domains reduces binding to Sos and negatively regulates downstream signaling pathways including Ras, JNK and MAPK. (rndsystems.com)
  • Not shown here is the activation under certain conditions of Jaks that are bound to some G-protein-coupled receptors (GPCRs) and the phosphorylation of STATs directly by certain ligand-activated growth factor receptors (RTKs) as well as non-receptor tyrosine kinases. (shu.edu)
  • Depending upon the receptor, IRS2 undergoes phosphorylation, either via Tyk2 following type I IFN binding, or via JAK1 and 3 following IL-4, -7 and -15 binding. (rndsystems.com)
  • Together with research on PTB domains of tensin1 and tensin2 it really is believed the fact that relationship of integrin β tails with PTB domains of cten and various other tensins is indie of tyrosine phosphorylation (Chen and Lo 2003 Calderwood Temocapril et al. (researchensemble.com)
  • non-etheless there are many exceptions like the SH2 domains of SLAM-associated proteins (aka SAP SH2D1A) and cten where the binding needs Temocapril the tyrosine but irrespective of its phosphorylation position. (researchensemble.com)
  • SH2 domains of cten and various other tensins bind towards the SIY442DNV site on DLC1 (Deleted in Liver organ Cancer tumor 1) and phosphorylation from the tyrosine is not needed (Liao et al. (researchensemble.com)
  • Upon tyrosine phosphorylation, insulin receptor substrate proteins interact with specific SH2 DOMAIN containing proteins that are involved in insulin receptor signaling. (bvsalud.org)
  • This gene encodes a scaffold protein that is thought to be involved in the regulation of the c-Jun amino-terminal kinase signaling pathway. (nih.gov)
  • Binding of phosphatidylinositol 3,4,5-trisphosphate to the pleckstrin homology domain of protein kinase B induces a conformational change. (cathdb.info)
  • We have identified a novel pathway that directs Lyn/Src family tyrosine kinase signals to the invadopodia to regulate sarcoma cell invasion via the molecule AFAP-1-like-1 (AFAP1L1), a new member of the AFAP (actin filament-associated protein) family. (nature.com)
  • AFAP1L1 intersects several invadopodia pathway components through its multiple domains and motifs, including the following (i) pleckstrin homology domains that bind phospholipids generated at the plasma membrane by phosphoinositide 3-kinase, (ii) a direct filamentous-actin binding domain and (iii) phospho-tyrosine motifs (pY136 and pY566) that specifically bind Vav2 and Nck2 SH2 domains, respectively. (nature.com)
  • In contrast, protein kinase C inhibition or depletion had no effect on BK-induced c-fos mRNA, AP-1-DNA binding activity, or DNA synthesis. (nih.gov)
  • Was this a function of differences in receptor primary sequence, their locations in the cell, or, possibly, the specificity of the protein kinase domain of the receptor? (the-scientist.com)
  • 1] J. Schlessinger and M. A. Lemmon, "SH2 and PTB domains in tyrosine kinase signaling. (chemdiv.com)
  • Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. (embl.de)
  • Pleckstrin, the protein where this domain was first detected, is the major substrate of protein kinase C in platelets. (embl.de)
  • The Src Homology 2 (SH2) domain is a major protein interaction module that is central to tyrosine kinase signaling. (eu.org)
  • An in vitro immunocomplex kinase assay indicated that the rpS3 protein acts as a substrate for Lyn, which phosphorylates the Y167 residue of rpS3. (bmbreports.org)
  • A Drosophila SH2-SH3 adaptor protein implicated in coupling the sevenless tyrosine kinase to an activator of Ras guanine nucleotide exchange, Sos. (wikidata.org)
  • Mutations in the tyrosine kinase, whether in BCR-ABL in CML or a FLT3 mutation in AML, bypass control that comes from ligand binding. (shu.edu)
  • C1: proteins kinase C conserved locations. (researchensemble.com)
  • A structurally-related group of signaling proteins that are phosphorylated by the INSULIN RECEPTOR PROTEIN-TYROSINE KINASE. (bvsalud.org)
  • The genome-wide search for disease-causing variations in the SH2 domains revealed eight genes: Bruton tyrosine kinase (BTK), SH2 domain-containing protein 1A (SH2D1A), Ras GTPase activating protein (RasGAP), tyrosine protein kinase Zap-70, SHP-2, the p85α subunit of the PIP3 kinase (PI3-K), signal transducer and activator of transcription 1α/β (STAT1) and STAT5B. (lu.se)
  • AD is pathologically characterized by the deposition of pathogenic Aβ peptides that are derived from larger integral membrane proteins, termed β-amyloid precursor proteins (APPs). (jneurosci.org)
  • Adam Kashishian (Fred Hutchinson Cancer Research Center, Seattle): "The question of the specificity of Src homology 2 (SH2) domain/phosphotyrosine interactions has been an important one since the ability of the SH2 domains to bind phosphotyrosine- containing peptides was first shown. (the-scientist.com)
  • Non-phosphorylated peptides do not bind to the SH2 domains. (eu.org)
  • B) Cten appearance is certainly induced by many growth elements and cytokines (shown in vibrant) through Ras-Mek-MAPK … Framework Human cten is certainly a 715-residue polypeptide which includes two conserved domains: the SH2 area and PTB area (Lo and Lo 2002 1 Both had been originally defined as binding modules for phosphotyrosine-containing peptides. (researchensemble.com)
  • The PTB domain interacts with the cytoplasmic tails of beta integrin by binding to an NPXY motif. (wikipedia.org)
  • To further define which neurons express Eph, antibodies were generated to the cytoplasmic portion of the Eph protein. (sdbonline.org)
  • Each subunit of IFNAR contains an N-terminal ligand binding domain (with two or four fibronectin type II-like subdomains, for IFNAR2 and IFNAR1, respectively), a transmembrane (TM) domain, and a cytoplasmic domain. (wikidoc.org)
  • It binds to phosphotyrosine in the cytoplasmic tail of cell surface receptors via its central SH2 domain, and to its immediate downstream target. (elsevierpure.com)
  • The protein encoded by this gene interacts with the cytoplasmic domains of amyloid beta (A4) precursor protein and amyloid beta (A4) precursor-like protein 2. (utsouthwestern.edu)
  • Among them are the Sprouty proteins which mainly act as inhibitors of growth factor-dependent neuronal and glial signaling pathways. (springer.com)
  • From studies of APP trafficking and metabolism, the following pathways have emerged: in the first, a fraction of APP molecules residing on the cell surface are processed by ADAM/TACE "sheddases" N-terminal to the ectodomain-transmembrane domain to generate an 83 aa membrane-tethered stub, termed α-CTF. (jneurosci.org)
  • The findings presented here indicate that CCM2 regulates protein complexes and signaling pathways important in endothelial cell function and provide insight into the molecular mechanisms involved in cerebral cavernous malformation pathogenesis. (unc.edu)
  • Intracellular signaling pathways that involve protein tyrosine kinases (PTKs) are critical for the control of most cellular processes. (chemdiv.com)
  • SH2 (Src homology region 2) and PTB (phosphotyrosine-binding) domains are small protein modules that mediate protein-protein interactions involved in many signal transduction pathways. (chemdiv.com)
  • The functions of SH2 and PTB domains include targeting of their host proteins to different cellular compartments, assembly of key components of signaling pathways in response to extracellular signals, and the control of autoinhibition, activation and dimerization of their host proteins. (chemdiv.com)
  • The SH3 domains associate with proline rich motifs on the guanine nucleotide releasing factor, Sos, stimulating GTP binding to Ras, which in turn activates MAPK and other signaling pathways. (rndsystems.com)
  • Involvement of SH2-containing phosphotyrosine phosphatase Syp in erythropoietin receptor signal transduction pathways. (drugbank.com)
  • The discovery of phosphotyrosine phosphatases that contain SH2 domains suggests roles for these molecules in growth factor signaling pathways. (drugbank.com)
  • 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)
  • Src Homology 2 (SH2) domains are small modular domains found within a great number of proteins involved in different signalling pathways. (eu.org)
  • [7] [8] Upon binding of type I interferons, IFNAR activates the JAK-STAT signalling pathway , along with MAPK , PI3K , and Akt signaling pathways. (wikidoc.org)
  • Adapter protein that functions as a negative regulator of many signaling pathways that start from receptors at the cell surface. (abcam.com)
  • The growth factor receptor-binding protein Grb2, composed of one SH2 and two SH3 domains, acts as an adaptor protein in transduction of signals from tyrosine-phosphorylaled proteins (EGF-receptor, or SHC), to the Ras dependent pathways. (elsevierpure.com)
  • This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analyzed to date. (cathdb.info)
  • Here we identify 93 SH2 domains from Legionella that are distinct in sequence and specificity from mammalian SH2 domains. (rcsb.org)
  • The Legionella SH2 domains feature the SH2 fold and a pTyr-binding pocket, but lack a specificity pocket found in a typical mammalian SH2 domain for recognition of sequences flanking the pTyr residue. (rcsb.org)
  • The human NCK1 (Nckα) and NCK2 (Nckβ/GRB4) SH2 domains show a degree of partner specificity but share the same mode of ligand binding ( Frese,2006 ) and belong to the class IA family which contains an aromatic residue (Phe) at the specificity-determining βD5 position ( Kaneko,2010 ). (eu.org)
  • Three loops surround the peptide binding pocket and are important for specificity: Because these loops can be flexible, considerable variation in peptide binding can apply for any given SH2 domain. (eu.org)
  • These ligands, having multiple binding portions, may be expected to bind with high affinity and specificity. (elsevierpure.com)
  • Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids. (embl.de)
  • After homogenization, the samples were submitted to differential centrifugation to obtain cell membranes and, further, to phospholipase C (PIPLC) treatment, to remove membrane-bound proteins anchored by phosphatidylinositol. (bvsalud.org)
  • The CCM2 phosphotyrosine binding (PTB) domain is necessary for a canonical interaction with NPxY motifs within CCM1. (unc.edu)
  • Cten's PTB area binds towards the NPXY theme from the integrin β1 tail (Katz et al. (researchensemble.com)
  • Both domains were initially identified as modules that recognize phosphorylated tyrosines in receptor tyrosine kinases and other signaling proteins. (chemdiv.com)
  • The proteins encoded by these genes have no apparent catalytic activity, suggesting they are scaffolds to organize and localize functional protein complexes in cells. (unc.edu)
  • Dimerized STATs then translocate to the nucleus, where they bind DNA in the promoter sequences of target genes to activate transcription. (medscape.com)
  • Using the Drosophila nephrocyte as a genetic screen platform, most genes involved in endocytosis and cell trafficking were screened, and the key components were identified of the cell trafficking pathway required for SD protein endocytosis and recycling. (sdbonline.org)
  • All genes in this SD protein endocytosis and recycling pathway, as well as SD proteins themselves, are highly conserved from flies to humans. (sdbonline.org)
  • Thus, these results suggest that the SD proteins in human kidney undergo the same endocytosis and recycling pathway to maintain the filtration structure, and mutations in any genes in this pathway could lead to abnormal SD and renal diseases. (sdbonline.org)
  • This domain occurred 3 times on human genes ( 3 proteins). (umbc.edu)
  • Thereafter, the STATs dimerize, each using its SH2 domain to bind to the phosphotyrosine of its partner, and then translocate to the nucleus, where they operate as transcription factors to activate expression of key genes, for example, the gene encoding an interferon. (shu.edu)
  • These phosphotyrosine motifs are essential for AFAP1L1-mediated cytoskeleton regulation. (nature.com)
  • They are able to bind specific motifs containing a phosphorylated tyrosine residue, propagating the signal downstream by promoting protein-protein interactions and/or modifying enzymatic activities. (eu.org)
  • Several different binding motifs are known, for example: pYEEI (Src-family SH2 domains), pY [IV]. (eu.org)
  • The C-terminal half of the SH2 domain exhibits greater structural variability and provides a platform for accommodating different kinds of SH2-binding motifs. (eu.org)
  • It contains Nterminalsites for myristylation and palmitylation, a PTK domain, and SH2 and SH3 domainswhich are involved in mediating protein-protein interactions with phosphotyrosine-containing andproline-rich motifs, respectively. (sciencepop.org)
  • It contains one PH (pleckstrin homology) domain (aa 16-144), followed by a PTB (phosphotyrosine-binding)domain (aa 194-298) and seven YxxM (Tyr/x/x/Met) motifs (aa 540-1075). (rndsystems.com)
  • This protein has been shown to interact with and regulate the activity of MAPK8/JNK1 and MAP2K7/MKK7 kinases. (nih.gov)
  • Our results suggest that a screening approach using protein crystallography is particularly useful to identify universal fragments for the conserved hydrophilic recognition sites found in target families such as SH2 domains, phosphatases, kinases, proteases, and esterases. (rcsb.org)
  • In general, Janus family tyrosine kinases (JAKs) bind to the intracellular components of cytokine receptors, and are, in turn, bound by STATs upon cytokine signaling. (medscape.com)
  • This mechanism is regulated by the activities of both protein-tyrosine kinases and protein tyrosine phosphatases. (drugbank.com)
  • 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)
  • The insulin receptor (IR) and JAK1 tyrosine kinases and STAT3 can serve as direct substrates for the T-cell protein tyrosine phosphatase (TCPTP). (diabetesjournals.org)
  • This gene is a member of the Src family of protein tyrosine kinases (PTKs). (sciencepop.org)
  • The Tir protein of EPEC binds NCK1/NCK2 SH2 domains through a high affinity pYDEV motif ( Frese,2006 ). (eu.org)
  • Our work expands the boundary of phosphotyrosine signalling to prokaryotes, suggesting that some bacterial effector proteins have acquired pTyr-superbinding characteristics to facilitate bacterium-host interactions. (rcsb.org)
  • In NCK SH2 domains, the EF loop is positioned away from the BG loop, exposing the pY+3 binding pocket where the side chain of Val forms tight interactions. (eu.org)
  • SH2 domains are phosphotyrosine recognition domains, often mediating transient interactions with target proteins. (eu.org)
  • No pairwise interactions are available for this conserved domain. (umbc.edu)
  • Furthermore, structural analysis of particular TM domains suggested locations for phenoxybenzamine covalent interactions. (pharmacology2000.com)
  • We found that Syp, a phosphotyrosine phosphatase, widely expressed in all tissues in mammals became phosphorylated on tyrosine after stimulation with Epo in M07ER cells engineered to express high levels of human EpoR. (drugbank.com)
  • The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. (antikoerper-online.de)
  • Src homology region 2 (SH2)-containing protein tyrosine phosphatase 2 (SHP2) is a nonreceptor phosphotyrosine phosphatase that promotes tumor progression in many types of cancer when activated by regulating the RAS signaling pathway. (scienceboard.net)
  • Here, we describe a method to detect microcystins in human plasma by using immunocapture followed by a protein phosphatase inhibition assay. (cdc.gov)
  • Fibroblast growth factor homologous factors are intracellular signaling proteins. (nih.gov)
  • The addition of an affinity tag allowed us to avoid the use of antibodies targeted toward the intracellular C-terminal tail of APP, a region to which a number of reported interacting proteins bind ( King and Turner, 2004 ). (jneurosci.org)
  • Disrupting any component in this pathway led to disrupted SD on the cell surface and intracellular accumulation of mislocalized SD proteins. (sdbonline.org)
  • These conserved regions appear to contain those structural elements needed for recognizing and binding various endogenous hormone/neurotransmitters (e.g. norepinephrine and epinephrine) as well as other ligands. (pharmacology2000.com)
  • Here, we describe an approach called ''consolidated" ligands to probe structural and functional activities of multidomain proteins. (elsevierpure.com)
  • The ligands with two binding portions can block simultaneously the one SH2 and one SH3, or two SH3 domains of Grb'2 with better than 100 nM affinity. (elsevierpure.com)
  • This study extends the feasibility of consolidated ligands, and this general protocol can be used to identify the interfaces between domains for rational design of higher affinity reagents. (elsevierpure.com)
  • For example, if a particular cysteine residue located in the TM3 domain was changed to valine (by mutation), the receptor becomes resistant to phenoxybenzamine inactivation. (pharmacology2000.com)
  • Mouse protein citron, a putative rho/rac effector that binds to the GTP-bound forms of rho and rac. (embl.de)
  • They usually appear in multidomain proteins, together with catalytic domains, or other protein binding modules, such as Src homology 3 (SH3), phosphotyrosine binding (PTB) or pleckstrin homology (PH) domains. (lu.se)
  • Membrane trafficking of G protein-coupled receptors (GPCRs) tightly orchestrates the signaling from this superfamily of signaling receptors. (frontiersin.org)
  • 8, 9] STAT3 is one of 7 human STAT (signal transducer and activator of transcription) proteins, which are critical second messengers for many cytokine, hormone, and growth factor receptors. (medscape.com)
  • Different growth factor receptors were known to bind different constellations of SH2 domain-containing proteins. (the-scientist.com)
  • The protein localizes to the plasma membrane andpericentrosomal vesicles, and binds to cell surface receptors, including CD4 and CD8, and othersignaling molecules. (sciencepop.org)
  • that is, of the 182 amino acids defining the TM domains of the human α 2A -adrenergic receptors, about 40% are identical with the human β 2 -adrenergic receptors. (pharmacology2000.com)
  • The binding affinity of an SH2 domain to a pTyr containing ligand is moderate, with the typical affinity range between 0.1 µМ to 10 µМ for equilibrium dissociation constant values (Kd) ( Kaneko,2012 ). (eu.org)
  • In the canonical mode of SH2 binding, regions on either side of the central β sheet are involved in ligand binding. (eu.org)
  • The α-adrenergic receptor is described by seven α-helical transmembrane (TM) domains which form a 'crevice' for ligand binding. (pharmacology2000.com)
  • Ligand binding to either subunit is required for and precedes dimerization and activation of the receptor. (wikidoc.org)
  • [7] Each type I IFN ligand contains a "hotspot", or a sequence of conserved amino acids that are involved in binding to the receptor, specifically the high affinity receptor IFNAR2, which determines the affinity of each ligand for the receptor. (wikidoc.org)
  • Structural analysis of type I IFN receptor with different type I IFN ligand subtypes revealed a similar binding site for the different agonists. (wikidoc.org)
  • A higher order consolidated ligand with three binding portions was developed and high affinity binding was achieved. (elsevierpure.com)
  • Insulin receptor substrate-1 proteins contain both a pleckstrin homology domain and a phosphotyrosine binding (PTB) domain. (wikipedia.org)
  • The VEE is a heterogeneous compartment containing the Adaptor Protein Phosphotyrosine Interacting with Pleckstrin homology Domain and Leucine Zipper 1 (APPL1) with distinct functions in regulating endosomal Gαs/cAMP signaling and rapid recycling. (frontiersin.org)
  • Pleckstrin homology domain. (embl.de)
  • Pleckstrin homology (PH) domains are small modular domains that occur in a large variety of proteins. (embl.de)
  • The proteins share an N-terminal PLECKSTRIN HOMOLOGY DOMAIN, a phosphotyrosine-binding domain that interacts with the phosphorylated INSULIN RECEPTOR, and a C-terminal TYROSINE-rich domain. (bvsalud.org)
  • 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)
  • Sos (a Ras guaninc nucleotide releasing factor), via its SH3 domains. (elsevierpure.com)
  • The screen for new phospho-tyrosine mimics binding to the SH2 domain of (pp60)src was initiated because of the limited cell penetration of phosphates. (rcsb.org)
  • This PTP contains two tandem Src homology-2 domains, which function as phospho-tyrosine binding domains and mediate the interaction of this PTP with its substrates. (antikoerper-online.de)
  • Tensin is a multi-domain protein that binds to actin filaments and functions as a focal-adhesion molecule (focal adhesions are regions of plasma membrane through which cells attach to the extracellular matrix). (wikipedia.org)
  • Through a novel CCM2 PTB domain - Smurf1 HECT domain interaction, CCM2 recruits Smurf1 to specific locations at the plasma membrane where it specifically degrades RhoA. (unc.edu)
  • This study provides the first in vivo evidence of trapped SD proteins in clathrin-coated pits at the plasma membrane when this pathway is disrupted. (sdbonline.org)
  • In an attempt to understand the function of APP, in vitro studies have focused on the identification of interacting proteins. (jneurosci.org)
  • Both NH2-terminal and COOH-terminal SH2 domains of Syp, made as glutathione S-transferase fusion proteins, were able to bind to the tyrosine-phosphorylated EpoR in vitro. (drugbank.com)
  • Human tensin has actin-binding sites, an SH2 (Pfam PF00017) domain and a region similar to the tumour suppressor PTEN. (wikipedia.org)
  • NCK is a major adaptor protein involved in membrane receptor signalling and modulation of actin cytoskeleton dynamics. (eu.org)
  • ABD: actin-binding area. (researchensemble.com)
  • To investigate the APP in vivo interactome in an unbiased manner, we generated mice that harbor a mouse prion protein promoter-driven cDNA encoding human APP-695 fused to a C-terminal affinity tag. (jneurosci.org)
  • Thus, this study demonstrates that using proteomic methods on our transgenic model can uncover important in vivo APP-interacting proteins that will provide insights into the biology of APP. (jneurosci.org)
  • Thus, this study demonstrates that our transgenic model can uncover important in vivo APP-interacting proteins that will contribute to our understanding of APP processing in in vivo settings. (jneurosci.org)
  • The phosphate group of Tyr is tightly bound in the conserved pTyr binding pocket. (eu.org)
  • The N-terminal region is most conserved and contains the pTyr binding pocket. (eu.org)
  • Comparison of the X-ray structures shows that the presence of the H-bond acceptors and not their relative position within the pharmacophore are essential for fragment binding and/or high affinity binding of full length inhibitors. (rcsb.org)
  • Val and Pro confer high-affinity binding at pY+3 - Ala and Ile are tolerated but confer weaker binding. (eu.org)
  • Differential roles of JIP scaffold proteins in the modulation of amyloid precursor protein metabolism. (nih.gov)
  • Aβ is liberated from type I integral membrane proteins, termed β-amyloid precursor proteins (APPs), by the concerted action of β-secretase (BACE1) and γ-secretase (for review, see Selkoe, 2002 ). (jneurosci.org)
  • The researchers discovered APPL1, a protein unrelated to amyloid precursor protein (APP) despite its similar acronym, directly links βCTF to a second protein, rab5, known to activate the molecular chain of events leading to neurodegeneration. (neurosciencenews.com)
  • Type I IFN binding to IFNAR1 was less strongly impacted by mutating single amino acids to alanine. (wikidoc.org)
  • There are actually three human α 2 -adrenoreceptor subtypes and the amino acid sequences between them are highly conserved within the seven hydrophobic TM domains. (pharmacology2000.com)
  • Here, we show that APP can coimmunoprecipitate NEEP21 from nontransgenic mouse brain and from mammalian cells stably coexpressing both proteins. (jneurosci.org)
  • Src homology 2 (SH2) domains play a critical role in signal transduction in mammalian cells by binding to phosphorylated Tyr (pTyr). (rcsb.org)
  • The phosphotyrosine-binding domain of insulin receptor substrate-1 is not related to the phosphotyrosine-binding domain of tensin. (wikipedia.org)
  • The PTB domains facilitate interaction with the activated tyrosine-phosphorylated insulin receptor. (wikipedia.org)
  • Ribosomal protein S3 (RpS3) is involved in protein biosynthesis as a component of the ribosome complex and possesses endonuclease activity to repair damaged DNA. (bmbreports.org)
  • PSPN not only binds GFRα4 but also signals in neurons mediated by GFRα1 [ 5 ]. (medsci.org)
  • The interferon-α/β receptor (IFNAR) is a virtually ubiquitous membrane receptor which binds endogenous type I interferon (IFN) cytokines. (wikidoc.org)
  • A PDGF receptor domain essential for mitogenesis but not for many other responses to PDGF. (wikidata.org)
  • SCOP: Structural Classification of Proteins and ASTRAL. (berkeley.edu)
  • CATH: Protein Structure Classification Database by I. Sillitoe, N. Dawson, T. Lewis, D. Lee, J. Lees, C. Orengo is licensed under a Creative Commons Attribution 4.0 International License . (cathdb.info)