1d8m

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Revision as of 14:24, 12 November 2007

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spinqualitylabelsall models 1d8m, resolution 2.44Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE OF MMP3 COMPLEXED WITH A HETEROCYCLE-BASED INHIBITOR

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

Potent and selective inhibition of matrix metalloproteinases was, demonstrated for a series of sulfonamide-based hydroxamic acids. The, design of the heterocyclic sulfonamides incorporates a six- or, seven-member central ring with a P2' substituent that can be modified., Binding interactions of this substituent at the S2' site are believed to, contribute to high inhibitory potency against stromelysin, collagenase-3, and gelatinases A and B, and to provide selectivity against collagenase-1, and matrilysin. An X-ray structure of a stromelysin inhibitor complex was, obtained to provide insights into the SAR and selectivity trends observed, for the series.

Disease

Known diseases associated with this structure: Coronary heart disease, susceptibility to OMIM:[185250]

About this Structure

1D8M is a Single protein structure of sequence from Homo sapiens with ZN, CA and BBH as ligands. Active as Stromelysin 1, with EC number 3.4.24.17 Full crystallographic information is available from OCA.

Reference

Heterocycle-based MMP inhibitors with P2' substituents., Pikul S, Dunham KM, Almstead NG, De B, Natchus MG, Taiwo YO, Williams LE, Hynd BA, Hsieh LC, Janusz MJ, Gu F, Mieling GE, Bioorg Med Chem Lett. 2001 Apr 23;11(8):1009-13. PMID:11327577

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