2src: Difference between revisions

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[[Image:2src.~~gif~~|left|200px]]

[[Image:2src.png|left|200px]]

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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.

==About this Structure==

2SRC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2SRC OCA].

~~==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://www.ncbi.nlm.nih.gov/pubmed/10360179 10360179]

[[Category: Homo sapiens]]

[[Category: Single protein]]

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[[Category: Src]]

[[Category: Tyrosine-protein kinase]]

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-[[Image:2src.gif|left|200px]]
+[[Image:2src.png|left|200px]]
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-==Overview==
+{{ABSTRACT_10360179}}
-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.
 ==About this Structure==
 SRC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2SRC OCA].
-==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://www.ncbi.nlm.nih.gov/pubmed/10360179 10360179]
 [[Category: Homo sapiens]]
 [[Category: Single protein]]
@@ Line 38: / Line 34: @@
 [[Category: Src]]
 [[Category: Tyrosine-protein kinase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 17:21:19 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jun 26 18:23:04 2008''