1HTD

STRUCTURAL INTERACTION OF NATURAL AND SYNTHETIC INHIBITORS WITH THE VENOM METALLOPROTEINASE, ATROLYSIN C (HT-D)

1HTD の概要

• エントリーDOI: 10.2210/pdb1htd/pdb
• 分子名称: ATROLYSIN C, ZINC ION, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: metalloprotease
• 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: 46505.48

構造登録者

Zhang, D.,Botos, I.,Gomis-Rueth, F.-X.,Doll, R.,Blood, C.,Njoroge, F.G.,Fox, J.W.,Bode, W.,Meyer, E.F. (登録日: 1994-01-20, 公開日: 1995-09-15, 最終更新日: 2024-10-30)

主引用文献

Zhang, D.,Botos, I.,Gomis-Ruth, F.X.,Doll, R.,Blood, C.,Njoroge, F.G.,Fox, J.W.,Bode, W.,Meyer, E.F.
Structural interaction of natural and synthetic inhibitors with the venom metalloproteinase, atrolysin C (form d).
Proc.Natl.Acad.Sci.USA, 91:8447-8451, 1994

PubMed Abstract: The structure of the metalloproteinase and hemorrhagic toxin atrolysin C form d (EC 3.4.24.42), from the venom of the western diamondback rattlesnake Crotalus atrox, has been determined to atomic resolution by x-ray crystallographic methods. This study illuminates the nature of inhibitor binding with natural (< Glu-Asn-Trp, where < Glu is pyroglutamic acid) and synthetic (SCH 47890) ligands. The primary specificity pocket is exceptionally deep; the nature of inhibitor and productive substrate binding is discussed. Insights gained from the study of these complexes facilitate the design of potential drugs to treat diseases where matrix metalloproteinases have been implicated, e.g., arthritis and tumor metastasis.

PubMed: 8078901
DOI: 10.1073/pnas.91.18.8447

実験手法

X-RAY DIFFRACTION (2.1 Å)