1MMP

MATRILYSIN COMPLEXED WITH CARBOXYLATE INHIBITOR

1MMP の概要

• エントリーDOI: 10.2210/pdb1mmp/pdb
• 分子名称: GELATINASE A, ZINC ION, CALCIUM ION, ... (5 entities in total)
• 機能のキーワード: metalloprotease
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Secreted, extracellular space, extracellular matrix (Probable): P09237
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 38788.90

構造登録者

Browner, M.F.,Smith, W.W.,Castelhano, A.L. (登録日: 1995-03-22, 公開日: 1996-04-03, 最終更新日: 2024-02-14)

主引用文献

Browner, M.F.,Smith, W.W.,Castelhano, A.L.
Matrilysin-inhibitor complexes: common themes among metalloproteases.
Biochemistry, 34:6602-6610, 1995

PubMed Abstract: Matrix metalloproteases are a family of enzymes that play critical roles in the physiological and pathological degradation of the extracellular matrix. These enzymes may be important therapeutic targets for the treatment of various diseases where tissue degradation is part of the pathology, such as cancer and arthritis. Matrilysin is the smallest member of this family of enzymes, all of which require zinc for catalytic activity. The first X-ray crystal structures of human matrilysin are presented. Inhibitors of metalloproteases are often characterized by the chemical group that interacts with the active site zinc of the protein. The structures of matrilysin complexed with hydroxamate (maximum resolution 1.9 A), carboxylate (maximum resolution 2.4 A), and sulfodiimine (maximum resolution 2.3 A) inhibitors are presented here and provide detailed information about how each functional group interacts with the catalytic zinc. Only the zinc-coordination group is variable in this series of inhibitors. Examination of these inhibitor-matrilysin complexes emphasizes the dominant role the zinc-coordinating group plays in determining the relative potencies of the inhibitors. The structures of these matrilysin-inhibitor complexes also provide a basis for comparing the catalytic mechanism of MMPs and other metalloproteins.

PubMed: 7756291
DOI: 10.1021/bi00020a004

実験手法

X-RAY DIFFRACTION (2.3 Å)