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Updated: Jul 10, 2026

Measurement of Factor V Activity in Human Plasma Using a Microplate Coagulation Assay
Published on: September 9, 2012
Proposed structural models of human factor Va and prothrombinase
C J Lee1, P Lin, V Chandrasekaran
1Department of Chemistry, UNC-CH, Chapel Hill, NC, USA.
Background:
The prothrombinase complex consists of factor Xa, FVa, calcium ions, and phospholipid membrane. The prothrombinase complex plays a key role in the blood coagulation process.
Objective:
To derive solvent-equilibrated models of human FVa and the prothrombinase complex.
Methods:
Several modeling techniques have been employed, including homology modeling, protein-protein docking, and molecular dynamics simulation methods, to build the structural models.
Results And Conclusions:
We found, upon simulation, a possibly significant shift towards planarity of the five FVa domains. To estimate a prothrombinase structure, we docked an FXa model to the equilibrated FVa model using experimental data as docking filters. We found that simulation of the docked complex led to some changes in the protein-protein contacts, but not buried surface area, as compared to the initial docking model. Possible locations of prothrombin binding to prothrombinase are indicated.
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