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1d0c

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(New page: 200px<br /><applet load="1d0c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1d0c, resolution 1.65Å" /> '''BOVINE ENDOTHELIAL N...)
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Revision as of 10:47, 20 November 2007

Image:1d0c.jpg

BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN COMPLEXED WITH 3-BROMO-7-NITROINDAZOLE (H4B FREE)

Overview

Nitric oxide is generated under normal and pathophysiological conditions, by three distinct isoforms of nitric oxide synthase (NOS). A, small-molecule inhibitor of NOS (3-Br-7-nitroindazole, 7-NIBr) is, profoundly neuroprotective in mouse models of stroke and Parkinson's, disease. We report the crystal structure of the catalytic heme domain of, endothelial NOS complexed with 7-NIBr at 1.65 A resolution. Critical to, the binding of 7-NIBr at the substrate site is the adoption by eNOS of an, altered conformation, in which a key glutamate residue swings out toward, one of the heme propionate groups. Perturbation of the heme propionate, ensues and eliminates the cofactor tetrahydrobiopterin-heme interaction., We also present three crystal structures that reveal how alterations at, the substrate site facilitate 7-NIBr and structurally dissimilar ligands, to occupy the cofactor site.

About this Structure

1D0C is a Single protein structure of sequence from Bos taurus with ACT, ZN, HEM, INE, CAD and GOL as ligands. Active as Nitric-oxide synthase, with EC number 1.14.13.39 Full crystallographic information is available from OCA.

Reference

Crystal structure of nitric oxide synthase bound to nitro indazole reveals a novel inactivation mechanism., Raman CS, Li H, Martasek P, Southan G, Masters BS, Poulos TL, Biochemistry. 2001 Nov 13;40(45):13448-55. PMID:11695891

Page seeded by OCA on Tue Nov 20 12:54:17 2007