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lüll Recent estimates of the structure of the factor VIIa (FVIIa)/tissue factor (TF) and factor Xa (FXa) ternary complex Lee CJ; Chandrasekaran V; Wu S; Duke RE; Pedersen LGThromb Res 2010[Apr]; 125 Suppl 1 (ä): S7-S10The 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.|1-Carboxyglutamic Acid/chemistry[MESH]|Algorithms[MESH]|Computer Simulation[MESH]|Epidermal Growth Factor/chemistry[MESH]|Factor VIIa/*chemistry[MESH]|Factor Xa/*chemistry[MESH]|Humans[MESH]|Models, Molecular[MESH]|Molecular Conformation[MESH]|Protein Conformation[MESH]|Protein Structure, Tertiary[MESH]|Thromboplastin/*chemistry[MESH] |