1P0S

Crystal Structure of Blood Coagulation Factor Xa in Complex with Ecotin M84R

1P0S の概要

• エントリーDOI: 10.2210/pdb1p0s/pdb
• 分子名称: Coagulation factor X precursor, Ecotin precursor, MAGNESIUM ION, ... (6 entities in total)
• 機能のキーワード: factor xa, serine protease, ecotin m84r, serine protease inhibitor, hydrolase
• 由来する生物種: Escherichia coli; 詳細
• 細胞内の位置: Secreted: P00742 P00742; Periplasm: P23827
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 60887.61

構造登録者

Wang, S.X.,Hur, E.,Sousa, C.A.,Brinen, L.,Slivka, E.J.,Fletterick, R.J. (登録日: 2003-04-10, 公開日: 2003-08-26, 最終更新日: 2021-10-27)

主引用文献

Wang, S.X.,Hur, E.,Sousa, C.A.,Brinen, L.,Slivka, E.J.,Fletterick, R.J.
The Extended Interactions and Gla Domain of Blood Coagulation Factor Xa
Biochemistry, 42:7959-7966, 2003

PubMed Abstract: The serine protease factor Xa (FXa) is inhibited by ecotin with picomolar affinity. The structure of the tetrameric complex of ecotin variant M84R (M84R) with FXa has been determined to 2.8 A. Substrate directed induced fit of the binding interactions at the S2 and S4 pockets modulates the discrimination of the protease. Specifically, the Tyr at position 99 of FXa changes its conformation with respect to incoming ligand, changing the size of the S2 and S4 pockets. The role of residue 192 in substrate and inhibitor recognition is also examined. Gln 192 from FXa forms a hydrogen bond with the P2 carbonyl group of ecotin. This confirms previous biochemical and structural analyses on thrombin and activated protein C, which suggested that residue 192 may play a more general role in mediating the interactions between coagulation proteases and their inhibitors. The structure of ecotin M84R-FXa (M84R-FXa) also reveals the structure of the Gla domain in the presence of Mg(2+). The first 11 residues of the domain assume a novel conformation and likely represent an intermediate folding state of the domain.

PubMed: 12834348
DOI: 10.1021/bi027320a

実験手法

X-RAY DIFFRACTION (2.8 Å)