2h9v
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(New page: 200px<br /><applet load="2h9v" size="450" color="white" frame="true" align="right" spinBox="true" caption="2h9v, resolution 3.100Å" /> '''Structural basis fo...)
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Revision as of 09:30, 21 November 2007
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Structural basis for induced-fit binding of Rho-kinase to the inhibitor Y27632
Overview
Rho-kinase is a main player in the regulation of cytoskeletal events and a, promising drug target in the treatment of both vascular and neurological, disorders. Here we report the crystal structure of the Rho-kinase, catalytic domain in complex with the specific inhibitor Y-27632., Comparison with the structure of PKA bound to this inhibitor revealed a, potential induced-fit binding mode that can be accommodated by the, phosphate binding loop. This binding mode resembles to that observed in, the Rho-kinase-fasudil complex. A structural database search indicated, that a pocket underneath the phosphate-binding loop is present that favors, binding to a small aromatic ring. Introduction of such a ring group might, spawn a new modification scheme of pre-existing protein kinase inhibitors, for improved binding capability.
About this Structure
2H9V is a Single protein structure of sequence from Bos taurus with Y27 as ligand. Active as Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 Full crystallographic information is available from OCA.
Reference
Structural basis for induced-fit binding of Rho-kinase to the inhibitor Y-27632., Yamaguchi H, Miwa Y, Kasa M, Kitano K, Amano M, Kaibuchi K, Hakoshima T, J Biochem (Tokyo). 2006 Sep;140(3):305-11. Epub 2006 Aug 4. PMID:16891330
Page seeded by OCA on Wed Nov 21 11:37:40 2007
