1cgl
From Proteopedia
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STRUCTURE OF THE CATALYTIC DOMAIN OF FIBROBLAST COLLAGENASE COMPLEXED WITH AN INHIBITOR
Overview
Collagenase is a zinc-dependent endoproteinase and is a member of the, matrix metalloproteinase (MMP) family of enzymes. The MMPs participate in, connective tissue remodeling events and aberrant regulation has been, associated with several pathologies. The 2.4 angstrom resolution structure, of the inhibited enzyme revealed that, in addition to the catalytic zinc, there is a second zinc ion and a calcium ion which play a major role in, stabilizing the tertiary structure of collagenase. Despite scant sequence, homology, collagenase shares structural homology with two other, endoproteinases, bacterial thermolysin and crayfish astacin. The detailed, description of protein-inhibitor interactions present in the structure, will aid in the design of compounds that selectively inhibit individual, members of the MMP family. Such inhibitors will be useful in examining the, function of MMPs in pathological processes.
About this Structure
1CGL is a Single protein structure of sequence from Homo sapiens with ZN and CA as ligands. Active as Interstitial collagenase, with EC number 3.4.24.7 Full crystallographic information is available from OCA.
Reference
Structure of the catalytic domain of fibroblast collagenase complexed with an inhibitor., Lovejoy B, Cleasby A, Hassell AM, Longley K, Luther MA, Weigl D, McGeehan G, McElroy AB, Drewry D, Lambert MH, et al., Science. 1994 Jan 21;263(5145):375-7. PMID:8278810
Page seeded by OCA on Tue Nov 20 12:25:57 2007
