2E3X

Crystal structure of Russell's viper venom metalloproteinase

2E3X の概要

• エントリーDOI: 10.2210/pdb2e3x/pdb
• 分子名称: Coagulation factor X-activating enzyme heavy chain, Coagulation factor X-activating enzyme light chain 2, Coagulation factor X-activating enzyme light chain 1, ... (9 entities in total)
• 機能のキーワード: disintegrin, metalloproteinase, c-type lectin, hydrolase, blood clotting, toxin
• 由来する生物種: Daboia russellii siamensis; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 80291.46

構造登録者

Igarashi, T.,Takeda, S. (登録日: 2006-11-30, 公開日: 2007-12-11, 最終更新日: 2024-10-23)

主引用文献

Takeda, S.,Igarashi, T.,Mori, H.
Crystal structure of RVV-X: an example of evolutionary gain of specificity by ADAM proteinases.
Febs Lett., 581:5859-5864, 2007

PubMed Abstract: Russell's viper venom factor X activator (RVV-X) is a heterotrimeric metalloproteinase with a mammalian ADAM-like heavy chain and two lectin-like light chains. The crystal structure of RVV-X has been determined at 2.9 A resolution and shows a hook-spanner-wrench-like architecture, in which the metalloproteinase/disintegrin region constitutes a hook, and the lectin-like domains constitute a handle. A 6.5nm separation between the catalytic site and a putative exosite suggests a docking model for factor X. The structure provides a typical example of the molecular evolution of multi-subunit proteins and insights into the molecular basis of target recognition and proteolysis by ADAM/adamalysin/reprolysin proteinases.

PubMed: 18060879
DOI: 10.1016/j.febslet.2007.11.062

実験手法

X-RAY DIFFRACTION (2.91 Å)