The crystal structure of the complex of blood coagulation factor VIIa with soluble tissue factor
DW Banner, A D'Arcy, C Chène, FK Winkler, A Guha… - Nature, 1996 - nature.com
DW Banner, A D'Arcy, C Chène, FK Winkler, A Guha, WH Konigsberg, Y Nemerson…
Nature, 1996•nature.comBlood coagulation is initiated when tissue factor binds to coagulation factor Vila to give an
enzymatically active complex which then activates factors IX and X, leading to thrombin
generation and clot formation. We have determined the crystal structure at 2.0-Å resolution
of active-site-inhibited factor VIIa complexed with the cleaved extracellular domain of tissue
factor. In the complex, factor VIIa adopts an extended conformation. This structure provides a
basis for understanding many molecular aspects of the initiation of coagulation.
enzymatically active complex which then activates factors IX and X, leading to thrombin
generation and clot formation. We have determined the crystal structure at 2.0-Å resolution
of active-site-inhibited factor VIIa complexed with the cleaved extracellular domain of tissue
factor. In the complex, factor VIIa adopts an extended conformation. This structure provides a
basis for understanding many molecular aspects of the initiation of coagulation.
Abstract
Blood coagulation is initiated when tissue factor binds to coagulation factor Vila to give an enzymatically active complex which then activates factors IX and X, leading to thrombin generation and clot formation. We have determined the crystal structure at 2.0-Å resolution of active-site-inhibited factor VIIa complexed with the cleaved extracellular domain of tissue factor. In the complex, factor VIIa adopts an extended conformation. This structure provides a basis for understanding many molecular aspects of the initiation of coagulation.
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