2tcl

From Proteopedia

Revision as of 15:42, 15 February 2008

STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN FIBROBLAST COLLAGENASE COMPLEXED WITH AN INHIBITOR

Overview

In rheumatoid and osteoarthritis, degradation of articular cartilage is, mediated by the matrix metalloproteinases collagenase, stromelysin and, gelatinase. The key event in this process is the cleavage of triple, helical collagen by collagenase. We have determined the crystal structure, of the catalytic domain of human recombinant fibroblast collagenase, complexed with a synthetic inhibitor at 2.2 A resolution. The protein fold, is similar to the amino termini of the zinc endopeptidases astacin, thermolysin and elastase despite a lack of primary sequence homology. The, conformation of the bound inhibitor provides a molecular basis for the, design of inhibitors of collagenase and other matrix metalloproteinases., Such inhibitors should be useful in the treatment of a variety of diseases, including arthritis and cancer.

Disease

Known diseases associated with this structure: COPD, rate of decline of lung function in OMIM:[120353]

About this Structure

2TCL is a Single protein structure of sequence from Homo sapiens with , , and as ligands. Full crystallographic information is available from OCA.

Reference

Structure of the catalytic domain of human fibroblast collagenase complexed with an inhibitor., Borkakoti N, Winkler FK, Williams DH, D'Arcy A, Broadhurst MJ, Brown PA, Johnson WH, Murray EJ, Nat Struct Biol. 1994 Feb;1(2):106-10. PMID:7656013

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