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Dynamic character of the complex of human blood coagulation factor VIIa with the extracellular domain of human tissue factor: a normal mode analysis
Author(s) -
Soejima Kenji,
Kurihara Youji,
Kamiya Kenshu,
Umeyama Hideaki
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)01564-1
Subject(s) - factor viia , tissue factor , chemistry , serine protease , factor vii , coagulation , cofactor , extracellular , biophysics , enzyme , biochemistry , protease , medicine , biology
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 Cα 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 Cα 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.