Presentation Title

Understanding the Role of the C2 Domain of Factor VIII in Platelet Membrane Binding

Presentation Type

Poster

Abstract

Blood coagulation factor VIII is a glycoprotein that binds to activated platelet membranes in the blood coagulation cascade to promote proper hemostasis. Nonfunctional factor VIII, largely characterized by the inability to bind activated platelet membranes, causes hemophilia A, a blood disorder that prevents blood clot formation. Understanding the binding mechanism of factor VIII to platelet phosphatidylserine membranes is essential in improving current hemophilia A therapeutics. Our research helps further the development of these therapeutics by analyzing the residue interactions between the C2 domain of factor VIII and phosphatidylserine membranes using ELISA binding studies and X-ray crystallography.

Comments

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Start Date

6-5-2017 12:15 PM

End Date

6-5-2017 2:00 PM

Location

Miller Hall

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May 6th, 12:15 PM May 6th, 2:00 PM

Understanding the Role of the C2 Domain of Factor VIII in Platelet Membrane Binding

Miller Hall

Blood coagulation factor VIII is a glycoprotein that binds to activated platelet membranes in the blood coagulation cascade to promote proper hemostasis. Nonfunctional factor VIII, largely characterized by the inability to bind activated platelet membranes, causes hemophilia A, a blood disorder that prevents blood clot formation. Understanding the binding mechanism of factor VIII to platelet phosphatidylserine membranes is essential in improving current hemophilia A therapeutics. Our research helps further the development of these therapeutics by analyzing the residue interactions between the C2 domain of factor VIII and phosphatidylserine membranes using ELISA binding studies and X-ray crystallography.