Abstract
Human coagulation factor V (FV) provides an essential function in the coagulation pathway. As a non-enzymatic cofactor of the prothrombinase complex, it is required for the rapid generation of thrombin [1, 2]. The gene for coagulation FV is located on chromosome 1q24.2 and spans more then 80 kilobases (kb) [3]. It consists of 25 exons encoding a 25 amino acids leader peptide and 2196 amino acids mature protein organized in A1-A2-B-A3-C1-C2 domain structure [4]. The activated factor Va is composed of a heavy chain (domains A1 and A2, Ala1-Arg709) and a light chain (domains A3, C1, and C2, Ser1546-Tyr2196), noncovalently associated in the presence of divalent metal ions.
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Delev, D., Pavlova, A., Seifried, E., Oldenburg, J. (2008). Structural Investigation of Two Novel Mutations in Coagulation Factor V by Molecular Modeling. In: Scharrer, I., Schramm, W. (eds) 37th Hemophilia Symposium. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-540-73535-9_49
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DOI: https://doi.org/10.1007/978-3-540-73535-9_49
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