1CGL

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

1CGL の概要

• エントリーDOI: 10.2210/pdb1cgl/pdb
• 関連するBIRD辞書のPRD_ID: PRD_000258
• 分子名称: FIBROBLAST COLLAGENASE, ZINC ION, CALCIUM ION, ... (5 entities in total)
• 機能のキーワード: metalloprotease, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 39412.46

構造登録者

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. (登録日: 1993-11-17, 公開日: 1995-02-27, 最終更新日: 2024-02-07)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.4 Å)