Factor VIIa-tissue factor interactions: an evaluation using factor VII-factor IX chimeras.
Using molecular biological techniques, a series of factor VII-factor IX chimeric molecules were made for both kinetic and competition binding assays to tissue factor in order to understand the interaction between factor VIIa and tissue factor. The results of the binding studies indicated that the major interaction between factor VIIa and tissue factor. The results of the binding studies indicated that the major interaction between factor VIIa and tissue factor involved both the first epidermal growth factor-like (EGF1) and catalytic domains of factor VII. In addition, both the gamma-carboxyglutamic acid-containing (Gla) and EGF2 domains also play a minor role in binding to tissue factor. The Gla and EGF-2 domain might either impart structure to the rest of the molecule or contribute a relatively small amount of energy to direct binding.
Chang
J Y
JY
Center for Thrombosis and Hemostasis, University of North Carolina at Chapel Hill 27599, USA.
D001667:Binding, Competitive; D001780:Blood Coagulation Tests; D005069:Evaluation Studies as Topic; D015942:Factor VIIa / Q000378:metabolism*; D006801:Humans; D007700:Kinetics; D017434:Protein Structure, Tertiary; D011993:Recombinant Fusion Proteins / Q000378:metabolism*; D013925:Thromboplastin / Q000378:metabolism*
D011993:Recombinant Fusion Proteins; D013925:Thromboplastin; D015942:Factor VIIa