3K65

Crystal Structure of Prethombin-2/Fragment-2 Complex

3K65 の概要

• エントリーDOI: 10.2210/pdb3k65/pdb
• 関連するPDBエントリー: 1HAG 2HPQ 3E6P
• 分子名称: Prothrombin, 1,4-BUTANEDIOL, ... (4 entities in total)
• 機能のキーワード: prothrombin, coagulation, zymogen, hydrolase
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Secreted, extracellular space: P00734 P00734
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 48191.22

構造登録者

Adams, T.E.,Huntington, J.A. (登録日: 2009-10-08, 公開日: 2010-09-29, 最終更新日: 2024-11-27)

主引用文献

Adams, T.E.,Huntington, J.A.
Structural transitions during prothrombin activation: On the importance of fragment 2.
Biochimie, 122:235-242, 2016

PubMed Abstract: Prothrombin is activated to thrombin by the prothrombinase complex through sequential cleavage at two distinct sites. This occurs at sites of vascular injury in a highly regulated cascade of serine protease and cofactor activation, where activated platelets provide a suitable surface for protease/cofactor/substrate assembly. The precise structural and conformational changes undergone during the transition from prothrombin to thrombin have been studied for decades, and several structures of prothrombin fragments along the activation pathway have been solved. Here we present a new structure analyzed in context of other recent structures and biochemical studies. What emerges is an unexpected mechanism that involves a change in the mode of binding of the F2 domain (fragment 2) on the catalytic domain after cleavage at Arg320, and a subsequent reorientation of the linker between the F2 and catalytic domain to present the Arg271 site for cleavage.

PubMed: 26365066
DOI: 10.1016/j.biochi.2015.09.013

実験手法

X-RAY DIFFRACTION (1.85 Å)