ArticleBiophysical journal2002
Structure and dynamics of zymogen human blood coagulation factor X.
Article in Biophysical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 83 citations in OpenAlex.
- Factor X M402T: a homozygous missense mutation identified as the cause of cross-reacting material-reduced deficiency.International journal of hematology · 2014Trial
- 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
- [Phylogenetic analysis and pathogenesis study of a new deletion mutation causing inherited FⅩ deficiency].Zhonghua xue ye xue za zhi = Zhonghua xueyexue zazhi · 2024Article
- Characteristics of FXa-storing platelets in hemophilia B mice and the influence of alcohol on the platelets.Scientific reports · 2023Article
- Unraveling the Reaction Mechanism of Russell's Viper Venom Factor X Activator: A Paradigm for the Reactivity of Zinc Metalloproteinases?Journal of chemical information and modeling · 2023Article
- Structural Model for Factor X Inhibition of IgM and Complement-Mediated Neutralization of Adenovirus.Viruses · 2023Article
- Lysyl oxidase-like 2 processing by factor Xa modulates its activity and substrate preference.Communications biology · 2023Article
- Comparative sequence analysis of vitamin K-dependent coagulation factors.Journal of thrombosis and haemostasis : JTH · 2022Article
- Unexpected Dynamic Binding May Rescue the Binding Affinity of Rivaroxaban in a Mutant of Coagulation Factor X.Frontiers in molecular biosciences · 2022Article
- Uncovering Membrane-Bound Models of Coagulation Factors by Combined Experimental and Computational Approaches.Thrombosis and haemostasis · 2021Review
- Activated factor X targeted stored in platelets as an effective gene therapy strategy for both hemophilia A and B.Clinical and translational medicine · 2021Article
- Alcohol functionality in the fatty acid backbone of sphingomyelin guides the inhibition of blood coagulation.RSC advances · 2021Article
- Serum Glycoproteomics and Identification of Potential Mechanisms Underlying Alzheimer's Disease.Behavioural neurology · 2021Article
- The Potential Role of Coagulation Factor Xa in the Pathophysiology of COVID-19: A Role for Anticoagulants as Multimodal Therapeutic Agents.TH open : companion journal to thrombosis and haemostasis · 2020Review
- Role of the activation peptide in the mechanism of protein C activation.Scientific reports · 2020Article
- Molecular mechanism of a novel Ser362Asn mutation causing inherited FX deficiency in a Chinese family.International journal of hematology · 2020Article
- Article
- A Phenome-Wide Association Study Uncovers a Pathological Role of Coagulation Factor X duringInfection and immunity · 2019Article
- Lipid specificity of the membrane binding domain of coagulation factor X.Journal of thrombosis and haemostasis : JTH · 2017Article
- Phosphatidylserine and FVa regulate FXa structure.The Biochemical journal · 2014Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The solution structure and dynamics of the human coagulation factor X (FX) have been investigated to understand the key structural elements in the zymogenic form that participates in the activation process. The model was constructed based on the 2.3-A-resolution x-ray crystallographic structure of active-site inhibited human FXa (PDB:1XKA). The missing gamma-carboxyglutamic acid (GLA) and part of epidermal growth factor 1 (EGF1) domains of the light chain were modeled based on the template of GLA-EGF1 domains of the tissue factor (TF)-bound FVIIa structure (PDB:1DAN). The activation peptide and other missing segments of FX were introduced using homology modeling. The full calcium-bound model of FX was subjected to 6.2 ns of molecular dynamics simulation in aqueous medium using the AMBER6.0 package. We observed significant reorientation of the serine-protease (SP) domain upon activation leading to a compact multi-domain structure. The solution structure of zymogen appears to be in a well-extended conformation with the distance between the calcium ions in the GLA domain and the catalytic residues estimated to be approximately 95 A in contrast to approximately 83 A in the activated form. The latter is in close agreement with fluorescence studies on FXa. The S1-specificity residues near the catalytic triad show significant differences between the zymogen and activated structures.
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