1sdd
Crystal Structure of Bovine Factor Vai
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OverviewOverview
In vertebrate hemostasis, factor Va serves as the cofactor in the, prothrombinase complex that results in a 300,000-fold increase in the rate, of thrombin generation compared with factor Xa alone. Structurally, little, is known about the mechanism by which factor Va alters catalysis within, this complex. Here, we report a crystal structure of protein C inactivated, factor Va (A1.A3-C1-C2) that depicts a previously uncharacterized domain, arrangement. This orientation has implications for binding to membranes, essential for function. A high-affinity calcium-binding site and a, copper-binding site have both been identified. Surprisingly, neither shows, a direct involvement in chain association. This structure represents the, largest physiologically relevant fragment of factor Va solved to date and, provides a new scaffold for the future generation of models of coagulation, cofactors.
About this StructureAbout this Structure
1SDD is a Protein complex structure of sequences from Bos taurus with NAG, NDG, CU and CA as ligands. Full crystallographic information is available from OCA.
ReferenceReference
The crystal structure of activated protein C-inactivated bovine factor Va: Implications for cofactor function., Adams TE, Hockin MF, Mann KG, Everse SJ, Proc Natl Acad Sci U S A. 2004 Jun 15;101(24):8918-23. Epub 2004 Jun 7. PMID:15184653
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