2src: Difference between revisions
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==About this Structure== | ==About this Structure== | ||
2SRC is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/ | 2SRC is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_Sapiens Homo Sapiens]] with ANP as [[http://en.wikipedia.org/wiki/ligand ligand]]. The following pages contain interesting information on the relation of 2SRC with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb60_1.html Ubiquitin]]. | ||
==Reference== | ==Reference== | ||
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10360179 10360179] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10360179 10360179] | ||
[[Category: Homo | [[Category: Homo Sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Src Tyrosine Kinase]] | [[Category: Src Tyrosine Kinase]] | ||
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[[Category: tyrosine-protein kinase]] | [[Category: tyrosine-protein kinase]] | ||
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Revision as of 18:49, 28 October 2007
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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 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 ... [(full description)]
About this StructureAbout this Structure
2SRC is a [Single protein] structure of sequence from [Homo Sapiens] with ANP as [ligand]. The following pages contain interesting information on the relation of 2SRC with [Ubiquitin].
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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