Phosphotyrosine binding domain
WebDec 19, 2014 · SH2D5 is a mammalian-specific, uncharacterized adaptor-like protein that contains an N-terminal phosphotyrosine-binding domain and a C-terminal Src homology 2 (SH2) domain. We show that SH2D5 is highly enriched in adult mouse brain, particularly in Purkinjie cells in the cerebellum and the cornu amm …
Phosphotyrosine binding domain
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WebThe Phosphotyrosine Binding (PTB) domain is one of the recently described domains involved in protein-protein interactions. WebNov 17, 1995 · This leads to the incorporation of MA molecules into virus cores, and subsequently into uncoated viral nucleoprotein complexes. A direct interaction between …
SH2 is conserved by signalization of protein tyrosine kinase, which are binding on phosphotyrosine (pTyr). In the human proteome the class of pTyr-selective recognition domains is represented by SH2 domains. The N-terminal SH2 domains of cytoplasmic tyrosine kinase was at the beginning of evolution evolved with the occurrence of tyrosine phosphorylation. At the beginning it was supposed that, these domains serve as a substrate for their target kinase. WebMar 13, 2008 · Surprisingly, despite the absence of a known phosphotyrosine-binding domain, pyruvate kinase exhibited a ≥15:1 SILAC heavy:light ratio, identifying it as a candidate novel...
WebThe F3 subdomain is a sandwich of two orthogonal antiparallel β sheets followed by an α helix; this fold is found in a number of structures, including the phosphotyrosine-binding … WebWe demonstrate that the phosphotyrosine binding domain of Shc is necessary and sufficient for its association with tyrosine-phosphorylated SHIP. Through site-directed mutagenesis, we have identified two tyrosines on SHIP, Tyr-917, and Tyr-1020, as the principal contact sites for the Shc- phosphotyrosine binding domain.
WebPhosphotyrosine (P.Tyr) residues on activated RTKs are recognized by a phosphodependent-binding domain, the SH2 domain. The recruitment of SH2 domain proteins to autophosphorylated RTKs at the plasma membrane is essential for initiating and propagating downstream signaling.
WebDec 7, 1995 · The PTB domain is structurally similar to pleckstrin homology domains (a β-sandwich capped by an α-helix) and binds to acidic phospholipids, suggesting a possible … green onions as a garnishIn molecular biology, Phosphotyrosine-binding domains are protein domains which bind to phosphotyrosine. The phosphotyrosine-binding domain (PTB, also phosphotyrosine-interaction or PI domain) in the protein tensin tends to be found at the C-terminus. Tensin is a multi-domain protein that binds to … See more APBA1; APBA2; APBA3; APPL1; EPS8; EPS8L1; EPS8L2; EPS8L3; TENC1; TNS; TNS1; TNS3; TNS4; DOK1; DOK2; DOK3; DOK4; DOK5; DOK6; DOK7; FRS2; FRS3; IRS1; IRS2; IRS4; NOS1AP; TLN1; TLN2 See more • SH2 domains also bind phosphorylated tyrosines See more • Eukaryotic Linear Motif resource motif class LIG_PTB_Phospho_1 See more green onions and scallionsWebMar 1, 2002 · Phosphotyrosine-binding (PTB) domains — also called phosphotyrosine-interacting domains ( PIDs) — were first identified in the SH2-domain-containing adaptor … green onions atkins inductionWebOct 6, 2006 · The RET receptor tyrosine kinase is important for several different biological functions during development. The recruitment at the phosphorylated Tyr1062 site in RET of a number of different … green onions bass tabWebThe phosphopeptide binding site is a bipartite pocket on the surface of the SH2 domain. One part of the pocket is lined by conserved basic amino acid residues and binds the … green onions at daryl\u0027s houseWebFeb 26, 2003 · These motifs are part of a canonical recognition sequence for phosphotyrosine-binding (PTB) domains, protein modules that are present in a wide variety of signaling and cytoskeletal proteins. Indeed, talin and ICAP1-α bind to integrin β tails by means of a PTB domain–NPXY ligand interaction. To assess the generality of this … flynas customer serviceWebMar 12, 1993 · A mouse phosphotyrosine phosphatase containing two Src homology 2 (SH2) domains, Syp, was identified. Syp bound to autophosphorylated epidermal growth factor (EGF) and platelet-derived growth factor (PDGF) receptors through its SH2 domains and was rapidly phosphorylated on tyrosine in PDGF- and EGF-stimulated cells. greenonions.botmanagerwindow