1DTH

METALLOPROTEASE

1DTH の概要

• エントリーDOI: 10.2210/pdb1dth/pdb
• 分子名称: ATROLYSIN C, ZINC ION, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: hydrolase, metalloprotease, zinc, venom
• 由来する生物種: Crotalus atrox (western diamondback rattlesnake)
• 細胞内の位置: Secreted: P15167
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 47717.02

構造登録者

Botos, I.,Scapozza, L.,Zhang, D.,Liotta, L.A.,Meyer, E.F. (登録日: 1996-02-12, 公開日: 1997-02-12, 最終更新日: 2024-10-30)

主引用文献

Botos, I.,Scapozza, L.,Zhang, D.,Liotta, L.A.,Meyer, E.F.
Batimastat, a potent matrix mealloproteinase inhibitor, exhibits an unexpected mode of binding.
Proc.Natl.Acad.Sci.USA, 93:2749-2754, 1996

PubMed Abstract: Matrix metalloproteinase enzymes have been implicated in degenerative processes like tumor cell invasion, metastasis, and arthritis. Specific metalloproteinase inhibitors have been used to block tumor cell proliferation. We have examined the interaction of batimastat (BB-94) with a metalloproteinase [atrolysin C (Ht-d), EC 3.4.24.42] active site at 2.0-angstroms resolution (R = 16.8%). The title structure exhibits an unexpected binding geometry, with the thiophene ring deeply inserted into the primary specificity site. This unprecedented binding geometry dramatizes the significance of the cavernous primary specificity site, pointing the way for the design of a new generation of potential antitumor drugs.

PubMed: 8610113
DOI: 10.1073/pnas.93.7.2749

実験手法

X-RAY DIFFRACTION (2 Å)