title: The interaction of activated factor VII with tissue factor: insight into the mechanism of cofactor-mediated activation of activated factor VII.
abstract: The structure solution of the complex of tissue factor (TF) and activated factor VII (FVIIa) and extensive mutagenesis analysis of the FVIIa protease domain have recently provided a detailed, novel insight into the function of the extrinsic activation complex. This overview relates the functional data to the known molecular interactions defined by crystallography, arriving at a hypothesis of how FVIIa is 'switched on' through specific contacts with TF. Combining these findings with the results of mutational analysis of TF, a picture emerges whereby multiple domains of both cofactor and enzyme provide contacts for the assembly of macromolecular substrate.
authors.affiliation: Department of Immunology, The Scripps Research Institute, La Jolla, CA 92037, USA. ruf@scripps.edu
authors.forename: W
authors.initials: W
authors.lastname: Ruf
mesh_terms: D000494:Allosteric Regulation; D004734:Energy Metabolism / Q000502:physiology; D015942:Factor VIIa / Q000378:metabolism*; D006801:Humans; D008958:Models, Molecular; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D013379:Substrate Specificity; D013925:Thromboplastin / Q000378:metabolism*
chemical_list: D013925:Thromboplastin; D015942:Factor VIIa