ArticleProceedings of the National Academy of Sciences of the United States of America2004
The crystal structure of activated protein C-inactivated bovine factor Va: Implications for cofactor function.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.
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Who cites it
63 citing papers in PubMed, 145 citations in OpenAlex.
- Cryogenic electron microscopy and coagulation factors.Current opinion in hematology · 2026Review
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- Article
- Elucidating the complex membrane binding of a protein with multiple anchoring domains using extHMMM.PLoS computational biology · 2024Article
- Copper-binding proteins and exonic splicing enhancers and silencers.Metallomics : integrated biometal science · 2024Article
- Membrane binding and lipid-protein interaction of the C2 domain from coagulation factor V.Current research in structural biology · 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
- Cryo-EM structure of coagulation factor V short.Blood · 2023Article
- The Magic of Proteases: From a Procoagulant and Anticoagulant Factor V to an Equitable Treatment of Its Inherited Deficiency.International journal of molecular sciences · 2023Review
- Cryo-EM structures of coagulation factors.Research and practice in thrombosis and haemostasis · 2022Review
- The Vascular Endothelium and Coagulation: Homeostasis, Disease, and Treatment, with a Focus on the Von Willebrand Factor and Factors VIII and V.International journal of molecular sciences · 2022Review
- Uncovering Membrane-Bound Models of Coagulation Factors by Combined Experimental and Computational Approaches.Thrombosis and haemostasis · 2021Review
- Prothrombinase: the paradigm for membrane bound enzyme complexes; a memoir.Journal of thrombosis and thrombolysis · 2021Review
- Article
- Factor VIII and Factor V Membrane Bound Complexes.Sub-cellular biochemistry · 2021Review
- Metal Binding Antimicrobial Peptides in Nanoparticle Bio-functionalization: New Heights in Drug Delivery and Therapy.Probiotics and antimicrobial proteins · 2020Review
- The 3.2 Å structure of a bioengineered variant of blood coagulation factor VIII indicates two conformations of the C2 domain.Journal of thrombosis and haemostasis : JTH · 2020Article
- Blood coagulation factor Va's key interactive residues and regions for prothrombinase assembly and prothrombin binding.Journal of thrombosis and haemostasis : JTH · 2019Review
- Understanding the Impact of Aberrant Splicing in Coagulation Factor V Deficiency.International journal of molecular sciences · 2019Article
3 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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.
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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.