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1cgl

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1cgl, resolution 2.40Å ()
Ligands: ,
Non-Standard Residues: , ,
Activity: Interstitial collagenase, with EC number 3.4.24.7
Domains: ZnMc_MMP
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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

Publication Abstract from PubMed

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.

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

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

1CGL is a 4 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

  • Lovejoy B, Cleasby A, Hassell AM, Longley K, Luther MA, Weigl D, McGeehan G, McElroy AB, Drewry D, Lambert MH, et al.. Structure of the catalytic domain of fibroblast collagenase complexed with an inhibitor. Science. 1994 Jan 21;263(5145):375-7. PMID:8278810

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