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Related Experiment Video

Updated: Jun 28, 2026

Measurement of Factor V Activity in Human Plasma Using a Microplate Coagulation Assay
13:08

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Published on: September 9, 2012

Modelling and expression studies of two novel mutations causing factor V deficiency.

Daniel Delev1, Anna Pavlova, Stefan Heinz

  • 1Institute of Experimental Haematology and Transfusion Medicine, University Clinic Bonn, Sigmund-Freud-Str. 25, 53127 Bonn, Germany. danidelev@yahoo.com

Thrombosis and Haemostasis
|November 8, 2008
PubMed
Summary

Two novel mutations in human coagulation factor V (FV) were identified, impacting thrombin generation. These FV variants, Tyr91Asn and Asp2098Tyr, alter protein structure and function, explaining bleeding disorder phenotypes.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Genetics

Background:

  • Human coagulation factor V (FV) is essential for thrombin generation, acting as a cofactor in the prothrombinase complex.
  • FV deficiency is a rare autosomal recessive bleeding disorder.
  • Understanding FV structure-function relationships is crucial for diagnosing and managing bleeding disorders.

Observation:

  • Two novel mutations, Tyr91Asn and Asp2098Tyr, were identified in patients with reduced FV activity (51% and 4%, respectively).
  • Molecular dynamics (MD) simulations and structural analysis were performed on these mutants.
  • Asp2098Tyr disrupted a conserved salt bridge in the C2 domain, affecting phospholipid-membrane binding.
  • Tyr91Asn induced conformational changes near the Cu(2+) binding site, potentially destabilizing FV chains.

Findings:

  • MD modeling indicated that Asp2098Tyr causes significant structural changes, including impaired phospholipid-membrane binding.
  • MD modeling suggested Tyr91Asn affects the stabilization of FV heavy and light chains.
  • Transient expression studies confirmed reduced FV activity: 26% for Asp2098Tyr and 56% for Tyr91Asn compared to wild-type FV.

Implications:

  • These mutations alter the structural integrity and functional activity of coagulation factor V.
  • The findings provide molecular explanations for the clinical phenotypes observed in patients with these novel FV mutations.
  • This research contributes to the understanding of FV structure-function and the molecular basis of bleeding disorders.