1g4k

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Revision as of 14:54, 12 November 2007

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spinqualitylabelsall models 1g4k, resolution 2.0Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

X-ray Structure of a Novel Matrix Metalloproteinase Inhibitor Complexed to Stromelysin

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

A new class of matrix metalloproteinase (MMP) inhibitors has been, identified by screening a collection of compounds against stromelysin. The, inhibitors, 2,4,6-pyrimidine triones, have proven to be potent inhibitors, of gelatinases A and B. An X-ray crystal structure of one representative, compound bound to the catalytic domain of stromelysin shows that the, compounds bind at the active site and ligand the active-site zinc. The, pyrimidine triones mimic substrates in forming hydrogen bonds to key, residues in the active site, and provide opportunities for placing, appropriately chosen groups into the S1' specificity pocket of MMPS: A, number of compounds have been synthesized and assayed against stromelysin, and the variations in potency are explained in terms of the binding mode, revealed in the X-ray crystal structure.

Disease

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

About this Structure

1G4K is a Single protein structure of sequence from Homo sapiens with ZN, CA, HQQ and GOL as ligands. Active as Stromelysin 1, with EC number 3.4.24.17 Full crystallographic information is available from OCA.

Reference

X-ray structure of a novel matrix metalloproteinase inhibitor complexed to stromelysin., Dunten P, Kammlott U, Crowther R, Levin W, Foley LH, Wang P, Palermo R, Protein Sci. 2001 May;10(5):923-6. PMID:11316871

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