ArticleScientific reports2018
Structure of prothrombin in the closed form reveals new details on the mechanism of activation.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 45 citations in OpenAlex.
- Molecular mechanism of cleavage at R271 during prothrombin activation revealed by cryo-EM.Blood · 2026Article
- In vivo targeting of open prothrombin with the monoclonal antibody POmAb results in anticoagulation without excessive bleeding.Journal of thrombosis and haemostasis : JTH · 2026Article
- Lupus anticoagulant and antiprothrombin antibodies: embracing the future.Journal of thrombosis and haemostasis : JTH · 2025Review
- Crystal structure of coagulation factor XII N-terminal domains 1-5.Acta crystallographica. Section D, Structural biology · 2025Article
- Article
- A model of zymogen factor XII: insights into protease activation.Blood advances · 2025Article
- Serious issues with cryo-EM structures of human prothrombinase.Open biology · 2025Review
- Conformation of factor Xa in solution revealed by single-molecule spectroscopy.Journal of thrombosis and haemostasis : JTH · 2024Article
- Understanding the difference between type I and type II antiprothrombin antibodies and their effect on activated protein C resistance.Journal of thrombosis and haemostasis : JTH · 2024Article
- Article
- The Prothrombin-Prothrombinase Interaction.Sub-cellular biochemistry · 2024Review
- Cryo-EM structure of coagulation factor V short.Blood · 2023Article
- Cryo-EM structures of coagulation factors.Research and practice in thrombosis and haemostasis · 2022Review
- Article
- Predicting protein-membrane interfaces of peripheral membrane proteins using ensemble machine learning.Briefings in bioinformatics · 2022Article
- A novel insight into mechanism of derangement of coagulation balance: interactions of quantum dots with coagulation-related proteins.Particle and fibre toxicology · 2022Article
- A Novel ELISA Assay for the Detection of Anti-Prothrombin Antibodies in Antiphospholipid Syndrome Patients at High Risk of Thrombosis.Frontiers in immunology · 2021Article
- Mechanisms of ligand binding.Biophysics reviews · 2020Review
- Zymogen and activated protein C have similar structural architecture.The Journal of biological chemistry · 2020Article
- The J-elongated conformation of βThe Journal of biological chemistry · 2020Article
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
The clotting factor prothrombin exists in equilibrium between closed and open conformations, but the physiological role of these forms remains unclear. As for other allosteric proteins, elucidation of the linkage between molecular transitions and function is facilitated by reagents stabilized in each of the alternative conformations. The open form of prothrombin has been characterized structurally, but little is known about the architecture of the closed form that predominates in solution under physiological conditions. Using X-ray crystallography and single-molecule FRET, we characterize a prothrombin construct locked in the closed conformation through an engineered disulfide bond. The construct: (i) provides structural validation of the intramolecular collapse of kringle-1 onto the protease domain reported recently; (ii) documents the critical role of the linker connecting kringle-1 to kringle-2 in stabilizing the closed form; and (iii) reveals novel mechanisms to shift the equilibrium toward the open conformation. Together with functional studies, our findings define the role of closed and open conformations in the conversion of prothrombin to thrombin and establish a molecular framework for prothrombin activation that rationalizes existing phenotypes associated with prothrombin mutations and points to new strategies for therapeutic intervention.
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