ArticleBlood2021
Cryo-EM structures of human coagulation factors V and Va.
Article in Blood, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 49 citations in OpenAlex.
- Protein-protein interaction disruption as a next-generation antithrombotic strategy.Journal of thrombosis and thrombolysis · 2026Review
- Cryogenic electron microscopy and coagulation factors.Current opinion in hematology · 2026Review
- [From structure to function: new developments in the interaction of coagulation factor Ⅴ with tissue factor pathway inhibitor α].Zhonghua xue ye xue za zhi = Zhonghua xueyexue zazhi · 2026Review
- Molecular mechanism of cleavage at R271 during prothrombin activation revealed by cryo-EM.Blood · 2026Article
- A Case Report of Non-Neutralizing Acquired Factor V Inhibitor Mimicking Deficiency: Diagnostic Challenges and Therapeutic Implications.Case reports in hematology · 2026Article
- 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
- Analyzing 6211 unique variants in the upgraded interactive FVIII web database reveals novel insights into hemophilia A.Blood vessels, thrombosis & hemostasis · 2025Article
- Article
- A Novel Human Anti-FV mAb as a Potential Tool for Diagnostic and Coagulation Inhibitory Approaches.International journal of molecular sciences · 2025Article
- Serious issues with cryo-EM structures of human prothrombinase.Open biology · 2025Review
- Exploring the Diversity and Function of Serine Proteases in Toxicofera Reptile Venoms: A Comprehensive Overview.Toxins · 2024Review
- Elucidating the complex membrane binding of a protein with multiple anchoring domains using extHMMM.PLoS computational biology · 2024Article
- Structural architecture of the acidic region of the B domain of coagulation factor V.Journal of thrombosis and haemostasis : JTH · 2024Article
- Membrane binding and lipid-protein interaction of the C2 domain from coagulation factor V.Current research in structural biology · 2024Article
- Factor V variants in bleeding and thrombosis.Research and practice in thrombosis and haemostasis · 2024Article
- The Prothrombin-Prothrombinase Interaction.Sub-cellular biochemistry · 2024Review
- Lactadherin's Multistate Binding Predicts Stable Membrane-Bound Conformations of Factors V and VIII's C Domains.Biochemistry · 2023Article
- New insight into the traditional model of the coagulation cascade and its regulation: illustrated review of a three-dimensional view.Research and practice in thrombosis and haemostasis · 2023Article
- Cryo-EM structure of coagulation factor V short.Blood · 2023Article
- Impaired factor V-related anticoagulant mechanisms and deep vein thrombosis associated with A2086D and W1920R mutations.Blood advances · 2023Article
Corrections and comments
- Commented on byFV/FVa revealed.2021
Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
Coagulation factor V (fV) is the precursor of fVa, which, together with fXa, Ca2+, and phospholipids, defines the prothrombinase complex and activates prothrombin in the penultimate step of the coagulation cascade. We solved the cryogenic electron microscopy (cryo-EM) structures of human fV and fVa at atomic (3.3 Å) and near-atomic (4.4 Å) resolution, respectively. The structure of fV reveals the entire A1-A2-B-A3-C1-C2 assembly, but with a surprisingly disordered B domain. The C1 and C2 domains provide a platform for interaction with phospholipid membranes and support the A1 and A3 domains, with the A2 domain sitting on top of them. The B domain is highly dynamic and visible only for short segments connecting to the A2 and A3 domains. The A2 domain reveals all sites of proteolytic processing by thrombin and activated protein C, a partially buried epitope for binding fXa, and fully exposed epitopes for binding activated protein C and prothrombin. Removal of the B domain and activation to fVa exposes the sites of cleavage by activated protein C at R306 and R506 and produces increased disorder in the A1-A2-A3-C1-C2 assembly, especially in the C-terminal acidic portion of the A2 domain that is responsible for prothrombin binding. Ordering of this region and full exposure of the fXa epitope emerge as necessary steps in the assembly of the prothrombin-prothrombinase complex. These structures offer molecular context for the function of fV and fVa and pioneer the analysis of coagulation factors by cryo-EM.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.