1htd

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Revision as of 14:41, 20 November 2007

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spinqualitylabelsall models 1htd, resolution 2.1Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

STRUCTURAL INTERACTION OF NATURAL AND SYNTHETIC INHIBITORS WITH THE VENOM METALLOPROTEINASE, ATROLYSIN C (HT-D)

Overview

The structure of the metalloproteinase and hemorrhagic toxin atrolysin C, form d (EC 3.4.24.42), from the venom of the western diamondback, rattlesnake Crotalus atrox, has been determined to atomic resolution by, x-ray crystallographic methods. This study illuminates the nature of, inhibitor binding with natural (< Glu-Asn-Trp, where < Glu is pyroglutamic, acid) and synthetic (SCH 47890) ligands. The primary specificity pocket is, exceptionally deep; the nature of inhibitor and productive substrate, binding is discussed. Insights gained from the study of these complexes, facilitate the design of potential drugs to treat diseases where matrix, metalloproteinases have been implicated, e.g., arthritis and tumor, metastasis.

About this Structure

1HTD is a Single protein structure of sequence from Crotalus atrox with ZN and CA as ligands. Active as Atrolysin C, with EC number 3.4.24.42 Full crystallographic information is available from OCA.

Reference

Structural interaction of natural and synthetic inhibitors with the venom metalloproteinase, atrolysin C (form d)., Zhang D, Botos I, Gomis-Ruth FX, Doll R, Blood C, Njoroge FG, Fox JW, Bode W, Meyer EF, Proc Natl Acad Sci U S A. 1994 Aug 30;91(18):8447-51. PMID:8078901

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