Recent Estimates of the Structure of the Factor VIIa (FVIIa)/Tissue Factor (TF) and Factor Xa (FXa) Ternary Complex

被引：9
|
作者：
Lee, Chang Jun [1 ]
Chandrasekaran, Vasu [2 ]
Wu, Sangwook [1 ]
Duke, Robert E. [1 ]
Pedersen, Lee G. [1 ]
机构：
[1] Univ N Carolina, Dept Chem, Chapel Hill, NC 27599 USA
[2] Novartis Inst Biomed Res, Cambridge, MA 02139 USA
来源：
THROMBOSIS RESEARCH | 2010年 / 125卷
基金：
美国国家科学基金会;
关键词：
Factor VIIa; Tissue factor; Factor Xa; ternary complex; Molecular Dynamics simulation; MOLECULAR-DYNAMICS SIMULATION; TISSUE FACTOR REGION; CELL-BASED MODEL; COAGULATION-FACTOR; QUATERNARY COMPLEX; RESIDUES LYS(165); FACTOR-IX; DOMAIN; ACTIVATION; INTERACTS;
D O I：
10.1016/j.thromres.2010.01.022
中图分类号：
R5 [内科学];
学科分类号：
1002 ; 100201 ;
摘要：
The putative structure of the Tissue Factor/Factor VIIa/Factor Xa (TF/FVIIa/FXa) ternary complex is reconsidered. Two independently derived docking models proposed in 2003 (one for our laboratory: CHeA and one from the Scripps laboratory: Ss) are dynamically equilibrated for over 10 ns in an electrically neutral solution using all-atom molecular dynamics. Although the dynamical models (CHeB and Se) differ in atomic detail, there are similarities in that TF is found to interact with the gamma-carboxyglutamic acid (Gla) and Epidermal Growth Factor-like 1 (EGF-1) domains of FXa, and FVIIa is found to interact with the Gla, EGF-2 and serine protease (SP) domains of FXa in both models. FVIIa does not interact with the FXa EGF-1 domain in Se and the EGF domains of FVIIa do not interact with FXa in the CHeB. Both models are consistent with experimentally suggested contacts between the SP domain of FVIIa with the EGF-2 and SP domains of FXa. (C) 2010 Elsevier Ltd. All rights reserved.
引用
收藏
页码：S7 / S10
页数：4
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