ArticleThe Journal of biological chemistry2008
Mapping of the factor Xa binding site on factor Va by site-directed mutagenesis.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 24 citations in OpenAlex.
- Molecular mechanism of cleavage at R271 during prothrombin activation revealed by cryo-EM.Blood · 2026Article
- Article
- Basic regions of factor V and tissue factor pathway inhibitor mediate heavy chain and acidic region interactions on factor V revealed by tethered chemical cleavage.Journal of thrombosis and haemostasis : JTH · 2025Article
- [Pedigree analysis of novel missense mutations causing hereditary coagulation factor Ⅴ deficiency].Zhonghua xue ye xue za zhi = Zhonghua xueyexue zazhi · 2024Article
- Analysis of 363 Genetic Variants in F5 via an Interactive Web Database Reveals New Insights into FV Deficiency and FV Leiden.TH open : companion journal to thrombosis and haemostasis · 2023Article
- Article
- Uncovering Membrane-Bound Models of Coagulation Factors by Combined Experimental and Computational Approaches.Thrombosis and haemostasis · 2021Review
- Blood coagulation factor Va's key interactive residues and regions for prothrombinase assembly and prothrombin binding.Journal of thrombosis and haemostasis : JTH · 2019Review
- Amino acid region 1000-1008 of factor V is a dynamic regulator for the emergence of procoagulant activity.The Journal of biological chemistry · 2013Article
- Restoring the procofactor state of factor Va-like variants by complementation with B-domain peptides.The Journal of biological chemistry · 2013Article
- Article
- A bipartite autoinhibitory region within the B-domain suppresses function in factor V.The Journal of biological chemistry · 2012Article
- Evolving methods for single nucleotide polymorphism detection: Factor V Leiden mutation detection.Journal of clinical laboratory analysis · 2011Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
Activated coagulation factor V functions as a cofactor to factor Xa in the conversion of prothrombin to thrombin. Based on the introduction of extra carbohydrate side chains in recombinant factor V, we recently proposed several regions in factor Va to be important for factor Xa binding. To further define which residues are important for factor Xa binding, we prepared fifteen recombinant factor V variants in which clusters of charged amino acid residues were mutated, mainly to alanines. The factor V variants were expressed in COS-1 cells, and their functional properties evaluated in a prothrombinase-based assay, as well as in a direct binding test. Four of the factor V variants, 501A/510A/511D, 501A/510A/511D/513A, 513A/577A/578A, and 501A/510A/511D/513A/577A/578A exhibited markedly reduced factor Xa-cofactor activity tested in the prothrombinase assay, and reduced binding affinity as judged by the direct binding assay. These factor Va variants were normally cleaved at Arg-506 by activated protein C, and the interaction between the factor Xa-factor Va complex and prothrombin was unaffected by the introduced mutations. Based on the integration of all available data, we propose a key factor Xa binding surface to be centered on Arg-501, Arg-510, Ala-511, Asp-513, Asp-577, and Asp-578 in the factor Va A2 domain. These residues form an elongated charged factor Xa binding cluster on the factor Va surface.
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