2src: Difference between revisions

Revision as of 12:44, 28 October 2007

CRYSTAL STRUCTURE OF HUMAN TYROSINE-PROTEIN KINASE C-SRC, IN COMPLEX WITH AMP-PNP

OverviewOverview

Src family kinases are maintained in an assembled, inactive conformation, by intramolecular interactions of their SH2 and SH3 domains. Full, catalytic activity requires release of these restraints as well as, phosphorylation of Tyr-416 in the activation loop. In previous structures, of inactive Src kinases, Tyr-416 and flanking residues are disordered. We, report here four additional c-Src structures in which this segment adopts, an ordered but inhibitory conformation. The ordered activation ... [(full description)]

About this StructureAbout this Structure

2SRC is a [Protein single] structure of sequence from [Homo sapiens] with ANP as [ligand].

ReferenceReference

Crystal structures of c-Src reveal features of its autoinhibitory mechanism., Xu W, Doshi A, Lei M, Eck MJ, Harrison SC, Mol Cell. 1999 May;3(5):629-38. PMID:10360179

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 ==Overview==
-Src family kinases are maintained in an assembled, inactive conformation, by intramolecular interactions of their SH2 and SH3 domains. Full, catalytic activity requires release of these restraints as well as, phosphorylation of Tyr-416 in the activation loop. In previous structures, of inactive Src kinases, Tyr-416 and flanking residues are disordered. We, report here four additional c-Src structures in which this segment adopts, an ordered but inhibitory conformation. The ordered activation loop forms, an alpha helix that stabilizes the inactive conformation of the kinase, domain, blocks the peptide substrate-binding site, and prevents Tyr-416, phosphorylation. Disassembly of the regulatory domains, induced by SH2 or, SH3 ligands, or by dephosphorylation of Tyr-527, could lead to exposure, and phosphorylation of Tyr-416.
+Src family kinases are maintained in an assembled, inactive conformation, by intramolecular interactions of their SH2 and SH3 domains. Full, catalytic activity requires release of these restraints as well as, phosphorylation of Tyr-416 in the activation loop. In previous structures, of inactive Src kinases, Tyr-416 and flanking residues are disordered. We, report here four additional c-Src structures in which this segment adopts, an ordered but inhibitory conformation. The ordered activation ... [[http://ispc.weizmann.ac.il/pmbin/getpm?10360179 (full description)]]
 ==About this Structure==
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 [[Category: tyrosine-protein kinase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Oct 28 10:24:28 2007''
+''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Oct 28 11:48:56 2007''