View source for 2src

[[Image:2src.gif|left|100px]]
<applet load="2src" size="450" color="white" frame="true" align="right" spinBox="true" 
caption="2src, resolution 1.5&Aring;" />
'''CRYSTAL STRUCTURE OF HUMAN TYROSINE-PROTEIN KINASE C-SRC, IN COMPLEX WITH AMP-PNP'''<br />

==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 ... [[http://ispc.weizmann.ac.il/pmbin/getpm?10360179 (full description)]]

==About this Structure==
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]]. 

==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]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Doshi, A.]]
[[Category: Eck, M.J.]]
[[Category: Harrison, S.C.]]
[[Category: Lei, M.]]
[[Category: Xu, W.]]
[[Category: ANP]]
[[Category: phosphorylation]]
[[Category: phosphotransferase]]
[[Category: phosphotyrosine]]
[[Category: proto-oncogene]]
[[Category: sh2]]
[[Category: sh3]]
[[Category: src]]
[[Category: tyrosine-protein kinase]]

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