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Structure Of Blood Coagulation Factor Viii In Complex With Anti-C2 Domain Inhibitory Antibody, Estelle K. Ronayne, Shaun C. Peters, Joseph Gish, Celena Wilson, H. Trent Spencer, Christopher B. Doering, Pete Lollar, P. Clint Spiegel Jr., Kenneth C. Childers
Structure Of Blood Coagulation Factor Viii In Complex With Anti-C2 Domain Inhibitory Antibody, Estelle K. Ronayne, Shaun C. Peters, Joseph Gish, Celena Wilson, H. Trent Spencer, Christopher B. Doering, Pete Lollar, P. Clint Spiegel Jr., Kenneth C. Childers
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Factor VIII (fVIII) is a procoagulant protein that binds to activated factor IX (fIXa) on platelet surfaces to form the intrinsic tenase complex. Due to the high immunogenicity of fVIII, generation of antibody inhibitors is a common occurrence in patients during hemophilia A treatment and spontaneously occurs in acquired hemophilia A patients. Non-classical antibody inhibitors, which block fVIII activation by thrombin and formation of the tenase complex, are the most common anti-C2 domain pathogenic inhibitors in hemophilia A murine models and have been identified in patient plasmas. In this study, we report on the X-ray crystal structure of a B …