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.
Start Date
6-5-2017 12:15 PM
End Date
6-5-2017 2:00 PM
Genre/Form
posters
Subjects - Topical (LCSH)
Hemophilia--Research; Blood coagulation factor VIII
Type
Event
Format
application/pdf
Language
English
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.
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