Phosphotyrosine binding domain
WebNumb is a membrane-associated, phosphotyrosine binding (PTB) domain-containing protein that functions as an intrinsic determinant of cell fate during Drosophila development. We … WebPhosphorylation may be viewed as a device to control the assembly of protein complexes, and thereby to regulate the dynamic behavior of the cell. Phospho-dependent interaction …
Phosphotyrosine binding domain
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WebProteins encoding phosphotyrosine binding (PTB) domains function as adaptors or scaffolds to organize the signaling complexes involved in wide-ranging physiological processes including neural development, immunity, tissue homeostasis and cell growth. Due to structural differences, PTB domains are divided into three groups represented by ... 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.
WebNov 7, 2012 · Phosphotyrosine signaling Intracellular communication is transmitted via networks of molecules that execute information transfer using protein-mediated … 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 …
WebFeb 26, 2003 · These motifs are part of a canonical recognition sequence for phosphotyrosine-binding (PTB) domains, protein modules that are present in a wide … WebMar 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.
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 …
WebMay 13, 2024 · Figure 1. Lipid-binding abilities of some SH2 domains may contribute to spatio-temporal coordination of tyrosine kinase signaling hub dynamics. Alternative … dark chocolate merlot cookiesWebSeveral other PI domains have been identified that may also have binding specificity for the NPXY motif. The terminology used at present to define these domains is unclear. The … bisento project bursting rageWebThe 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 … bisento from blox fruitsWebMar 29, 2024 · The phosphotyrosine interaction (PI) domains (also known as the PTB, or phosphotyrosine binding, domains) of Shc and IRS-1 are recently described domains that … bisento drop rate king legacyWebMar 16, 2024 · Tyrosine kinases and SH2 (phosphotyrosine recognition) domains have binding specificities that depend on the amino acid sequence surrounding the target (phospho)tyrosine residue. bisento rarityWebOct 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 … bisento project new worldWebApr 27, 2016 · National Center for Biotechnology Information dark chocolate matcha green tea