2TCL

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

2TCL の概要

• エントリーDOI: 10.2210/pdb2tcl/pdb
• 分子名称: FIBROBLAST COLLAGENASE, ZINC ION, SAMARIUM (III) ION, ... (6 entities in total)
• 機能のキーワード: hydrolase (metalloprotease)
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Secreted, extracellular space, extracellular matrix (Probable): P03956
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19628.37

構造登録者

Winkler, F.K.,Borkakoti, N.,D'Arcy, A. (登録日: 1994-09-07, 公開日: 1996-03-08, 最終更新日: 2024-02-21)

主引用文献

Borkakoti, N.,Winkler, F.K.,Williams, D.H.,D'Arcy, A.,Broadhurst, M.J.,Brown, P.A.,Johnson, W.H.,Murray, E.J.
Structure of the catalytic domain of human fibroblast collagenase complexed with an inhibitor.
Nat.Struct.Biol., 1:106-110, 1994

PubMed Abstract: 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.

PubMed: 7656013
DOI: 10.1038/nsb0294-106

実験手法

X-RAY DIFFRACTION (2.2 Å)