2fci | pdb_00002fci

Structural basis for the requirement of two phosphotyrosines in signaling mediated by Syk tyrosine kinase

spinqualitylabelsall models 2fci Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2fci is a 2 chain structure with sequence from Bos taurus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Ligands: ACE, GMA, PTR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q32PK0_BOVIN Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The protein-tyrosine kinase Syk couples immune recognition receptors to multiple signal transduction pathways, including the mobilization of calcium and the activation of NFAT. The ability of Syk to regulate signaling is influenced by its phosphorylation on tyrosine residues within the linker B region. The phosphorylation of both Y342 and Y346 is necessary for optimal signaling from the B cell receptor for antigen. The SH2 domains of multiple signaling proteins share the ability to bind this doubly phosphorylated site. The NMR structure of the C-terminal SH2 domain of PLCgamma (PLCC) bound to a doubly phosphorylated Syk peptide reveals a novel mode of phosphotyrosine recognition. PLCC undergoes extensive conformational changes upon binding to form a second phosphotyrosine-binding pocket in which pY346 is largely desolvated and stabilized through electrostatic interactions. The formation of the second binding pocket is distinct from other modes of phosphotyrosine recognition in SH2-protein association. The dependence of signaling on simultaneous phosphorylation of these two tyrosine residues offers a new mechanism to fine-tune the cellular response to external stimulation. Structural basis for the requirement of two phosphotyrosine residues in signaling mediated by Syk tyrosine kinase.,Groesch TD, Zhou F, Mattila S, Geahlen RL, Post CB J Mol Biol. 2006 Mar 10;356(5):1222-36. Epub 2005 Dec 27. PMID:16410013 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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