title: Dynamic character of the complex of human blood coagulation factor VIIa with the extracellular domain of human tissue factor: a normal mode analysis.
abstract: As an attempt to investigate the dynamic interactions between plasma serine protease, coagulation factor VIIa (VIIa) and its cofactor, tissue factor (TF), we performed normal mode analysis (NMA) of the complex of VIIa with soluble TF (the extracellular part of TF; sTF). We compared fluctuations of Calpha atoms of VIIa or sTF derived from NMA in the VIIa-sTF complex with those of VIIa or sTF in an uncomplexed condition. The atomic fluctuations of the Calpha atoms of sTF complexed with VIIa did not significantly differ from those of sTF without VIIa. In contrast, the atomic fluctuations of VIIa complexed with sTF were much smaller than those of VIIa without sTF. These results suggest that domain motions of VIIa molecule alone are markedly dampened in the VIIa-sTF complex and that the sTF molecule is relatively more rigid than the VIIa molecule. This may indicate functions of TF as a cofactor.
authors.affiliation: First Research Department, Chemo-Sero-Therapeutic Research Institute, Kawabe, Kyokushi-mura, Kikuchi-gun, Kumamoto, Japan. soejima@kaketsuken.or.jp
authors.forename: K
authors.initials: K
authors.lastname: Soejima
authors.forename: Y
authors.initials: Y
authors.lastname: Kurihara
authors.forename: K
authors.initials: K
authors.lastname: Kamiya
authors.forename: H
authors.initials: H
authors.lastname: Umeyama
mesh_terms: D000596:Amino Acids / Q000737:chemistry; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D015942:Factor VIIa / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D008024:Ligands; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D011487:Protein Conformation; D013925:Thromboplastin / Q000737:chemistry* / Q000378:metabolism
chemical_list: D000596:Amino Acids; D008024:Ligands; D013925:Thromboplastin; D015942:Factor VIIa