1SDD

Crystal Structure of Bovine Factor Vai

1SDD の概要

• エントリーDOI: 10.2210/pdb1sdd/pdb
• 関連するPDBエントリー: 1CZS 1CZT 1CZV
• 分子名称: Coagulation factor V, 2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION, ... (6 entities in total)
• 機能のキーワード: coagulation, copper-binding protein, cofactor, blood clotting
• 由来する生物種: Bos taurus (cattle); 詳細
• 細胞内の位置: Secreted: Q28107 Q28107
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 110651.48

構造登録者

Adams, T.E.,Hockin, M.F.,Mann, K.G.,Everse, S.J. (登録日: 2004-02-13, 公開日: 2004-06-29, 最終更新日: 2024-11-20)

主引用文献

Adams, T.E.,Hockin, M.F.,Mann, K.G.,Everse, S.J.
The crystal structure of activated protein C-inactivated bovine factor Va: Implications for cofactor function.
Proc.Natl.Acad.Sci.USA, 101:8918-8923, 2004

PubMed Abstract: In vertebrate hemostasis, factor Va serves as the cofactor in the prothrombinase complex that results in a 300,000-fold increase in the rate of thrombin generation compared with factor Xa alone. Structurally, little is known about the mechanism by which factor Va alters catalysis within this complex. Here, we report a crystal structure of protein C inactivated factor Va (A1.A3-C1-C2) that depicts a previously uncharacterized domain arrangement. This orientation has implications for binding to membranes essential for function. A high-affinity calcium-binding site and a copper-binding site have both been identified. Surprisingly, neither shows a direct involvement in chain association. This structure represents the largest physiologically relevant fragment of factor Va solved to date and provides a new scaffold for the future generation of models of coagulation cofactors.

PubMed: 15184653
DOI: 10.1073/pnas.0403072101

実験手法

X-RAY DIFFRACTION (2.8 Å)