3GIS

Crystal Structure of Na-free Thrombin in Complex with Thrombomodulin

3GIS の概要

• エントリーDOI: 10.2210/pdb3gis/pdb
• 分子名称: Prothrombin, Thrombomodulin, SULFATE ION, ... (6 entities in total)
• 機能のキーワード: protein-protein complex, coagulation, acute phase, blood coagulation, cleavage on pair of basic residues, disease mutation, disulfide bond, gamma-carboxyglutamic acid, glycoprotein, hydrolase, kringle, protease, secreted, serine protease, zymogen, egf-like domain, hydroxylation, membrane, receptor, thrombophilia, transmembrane, blood clotting
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Secreted, extracellular space: P00734 P00734; Membrane; Single-pass type I membrane protein: P07204
• タンパク質・核酸の鎖数: 9
• 化学式量合計: 146571.21

構造登録者

Adams, T.E.,Huntington, J.A. (登録日: 2009-03-06, 公開日: 2009-08-18, 最終更新日: 2024-10-30)

主引用文献

Adams, T.E.,Li, W.,Huntington, J.A.
Molecular basis of thrombomodulin activation of slow thrombin
J.Thromb.Haemost., 7:1688-1695, 2009

PubMed Abstract: Coagulation is a highly regulated process where the ability to prevent blood loss after injury is balanced against the maintenance of blood fluidity. Thrombin is at the center of this balancing act. It is the critical enzyme for producing and stabilizing a clot, but when complexed with thrombomodulin (TM) it is converted to a powerful anticoagulant. Another cofactor that may play a role in determining thrombin function is the monovalent cation Na(+). Its apparent affinity suggests that half of the thrombin generated is in a Na(+)-free 'slow' state and half is in a Na(+)-coordinated 'fast' state. While slow thrombin is a poor procoagulant enzyme, when complexed to TM it is an effective anticoagulant.

PubMed: 19656282
DOI: 10.1111/j.1538-7836.2009.03563.x

実験手法

X-RAY DIFFRACTION (2.4 Å)