1CGL

Structure of the catalytic domain of fibroblast collagenase complexed with an inhibitor

Summary for 1CGL

• Entry DOI: 10.2210/pdb1cgl/pdb
• Related PRD ID: PRD_000258
• Descriptor: FIBROBLAST COLLAGENASE, ZINC ION, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: metalloprotease, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 39412.46

Authors

Lovejoy, B.,Cleasby, A.,Hassell, A.M.,Longley, K.,Luther, M.A.,Weigl, D.,Mcgeehan, G.,Mcelroy, A.B.,Drewry, D.,Lambert, M.H.,Jordan, S.R. (deposition date: 1993-11-17, release date: 1995-02-27, Last modification date: 2024-02-07)

Primary citation

Lovejoy, B.,Cleasby, A.,Hassell, A.M.,Longley, K.,Luther, M.A.,Weigl, D.,McGeehan, G.,McElroy, A.B.,Drewry, D.,Lambert, M.H.,Jordan, S.R.
Structure of the catalytic domain of fibroblast collagenase complexed with an inhibitor.
Science, 263:375-377, 1994

PubMed Abstract: 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.

PubMed: 8278810

Experimental method

X-RAY DIFFRACTION (2.4 Å)