ArticleBiochemical and biophysical research communications2014
Structural insights into the interaction of blood coagulation co-factor VIIIa with factor IXa: a computational protein-protein docking and molecular dynamics refinement study.
Article in Biochemical and biophysical research communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 33 citations in OpenAlex.
- Integrating Network Pharmacology, Machine Learning, and Experimental Validation to Elucidate the Mechanism of Cardamonin in Treating Idiopathic Pulmonary Fibrosis.International journal of molecular sciences · 2025Article
- The Construction of a Molecular Model for the Ternary Protein Complex of Intrinsic Coagulation Pathway Factors Provides Novel Insights for the Pathogenesis of Cross-Reactive Material Positive Coagulation Factor Mutations.International journal of molecular sciences · 2025Article
- Blood Coagulation Factor IX: Structure, Function, and Regulation.IUBMB life · 2025Review
- Review
- Heyde Syndrome Unveiled: A Case Report with Current Literature Review and Molecular Insights.International journal of molecular sciences · 2024Review
- SAXS analysis of the intrinsic tenase complex bound to a lipid nanodisc highlights intermolecular contacts between factors VIIIa/IXa.Blood advances · 2022Article
- The Molecular Basis of FIX Deficiency in Hemophilia B.International journal of molecular sciences · 2022Review
- A Machine Learning Framework Predicts the Clinical Severity of Hemophilia B Caused by Point-Mutations.Frontiers in bioinformatics · 2022Article
- A proximity-based in silico approach to identify redox-labile disulfide bonds: The example of FVIII.PloS one · 2022Article
- Article
- Exosites expedite blood coagulation.The Journal of biological chemistry · 2020Article
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
Coagulation factor X (FX) zymogen activation by factor IXa (FIXa) enzyme plays a critical role in the middle-phase of coagulation cascade. The activation process is catalytically inert and requires FIXa binding and complex formation with co-factor VIIIa (FVIIIa). In order to understand the structural details of the FVIIIa:FIXa complex, we employed knowledge-driven protein-protein docking and aqueous-phase MD refinement methods to develop a stable structural complex between FVIIIa and FIXa. The model shows that all four domains of FIXa wrap across FVIIIa that spans the co-factor binding surface of A2, A3 and C1 domains. The region surrounding the 558-helix of the A2-domain of FVIIIa is predicted to be the key interaction site with the helical segments of Lys293-Lys301 and Asp332-Arg338 residues of the serine-protease domain of FIXa. The hydrophobic helical stack between the GLA and EGF1 domains of FIXa is predicted to be primary interacting region with the A3-C2 domain interface of FVIIIa.
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Registered trials
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