1SDD

Crystal Structure of Bovine Factor Vai

Summary for 1SDD

• Entry DOI: 10.2210/pdb1sdd/pdb
• Related: 1CZS 1CZT 1CZV
• Descriptor: Coagulation factor V, 2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION, ... (6 entities in total)
• Functional Keywords: coagulation, copper-binding protein, cofactor, blood clotting
• Biological source: Bos taurus (cattle); More
• Cellular location: Secreted: Q28107 Q28107
• Total number of polymer chains: 2
• Total formula weight: 110651.48

Authors

Adams, T.E.,Hockin, M.F.,Mann, K.G.,Everse, S.J. (deposition date: 2004-02-13, release date: 2004-06-29, Last modification date: 2020-07-29)

Primary citation

Adams, T.E.,Hockin, M.F.,Mann, K.G.,Everse, S.J.
The crystal structure of activated protein C-inactivated bovine factor Va: Implications for cofactor function.
Proc.Natl.Acad.Sci.USA, 101:8918-8923, 2004

PubMed Abstract: 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.

PubMed: 15184653
DOI: 10.1073/pnas.0403072101

Experimental method

X-RAY DIFFRACTION (2.8 Å)