Solution structure of the N-terminal EGF-like domain from human factor VII.

@article{Muranyi1998SolutionSO,
  title={Solution structure of the N-terminal EGF-like domain from human factor VII.},
  author={Andreas Muranyi and Bryan E. Finn and Garry Gippert and Sture Fors{\'e}n and Johan Stenflo and Torbjorn Drakenberg},
  journal={Biochemistry},
  year={1998},
  volume={37 30},
  pages={10605-15}
}
Blood coagulation is initiated by Ca(2+)-dependent binding of coagulation factor VIIa (FVIIa) to its cofactor, tissue factor (TF). The TF:FVIIa complex activates factors IX and X, ultimately leading to the formation of thrombin and the coagulation of blood. FVII consists of an N-terminal gamma-carboxyglutamic-acid-containing (Gla) domain followed by two epidermal growth factor (EGF) like domains, the first of which can bind one Ca2+ ion (Kd approximately 150 microM) and a C-terminal serine… CONTINUE READING

From This Paper

Topics from this paper.

Similar Papers

Loading similar papers…