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2hvx
From Proteopedia
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(New page: 200px<br /> <applet load="2hvx" size="450" color="white" frame="true" align="right" spinBox="true" caption="2hvx, resolution 2.600Å" /> '''Discovery of Poten...)
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Revision as of 20:30, 12 November 2007
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Discovery of Potent, Orally Active, Nonpeptide Inhibitors of Human Mast Cell Chymase by Using Structure-Based Drug Design
Overview
A series of beta-carboxamido-phosphon(in)ic acids (2) was identified as a, new structural motif for obtaining potent inhibitors of human mast cell, chymase. For example, 1-naphthyl derivative 5f had an IC50 value of 29 nM, and (E)-styryl derivative 6g had an IC50 value of 3.5 nM. An X-ray, structure for 5f.chymase revealed key interactions within the enzyme, active site. Compound 5f was selective for inhibiting chymase versus eight, serine proteases. Compound 6h was orally bioavailable in rats (F=39%), and, orally efficacious in a hamster model of inflammation.
About this Structure
2HVX is a Single protein structure of sequence from Homo sapiens with DRX as ligand. Active as Chymase, with EC number 3.4.21.39 Full crystallographic information is available from OCA.
Reference
Discovery of potent, selective, orally active, nonpeptide inhibitors of human mast cell chymase., Greco MN, Hawkins MJ, Powell ET, Almond HR Jr, de Garavilla L, Hall J, Minor LK, Wang Y, Corcoran TW, Di Cera E, Cantwell AM, Savvides SN, Damiano BP, Maryanoff BE, J Med Chem. 2007 Apr 19;50(8):1727-30. Epub 2007 Mar 16. PMID:17361995
Page seeded by OCA on Mon Nov 12 22:37:10 2007
