ArticleThe Journal of biological chemistry2016
Structural Architecture of Prothrombin in Solution Revealed by Single Molecule Spectroscopy.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 42 citations in OpenAlex.
- Molecular mechanism of cleavage at R271 during prothrombin activation revealed by cryo-EM.Blood · 2026Article
- Prothrombinase processivity is conferred by substrate allostery.The EMBO journal · 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
- Regulation of histones in thromboinflammation.Frontiers in immunology · 2026Review
- Lupus anticoagulant and antiprothrombin antibodies: embracing the future.Journal of thrombosis and haemostasis : JTH · 2025Review
- The strand exchange domain of tumor suppressor PALB2 is intrinsically disordered and promotes oligomerization-dependent DNA compaction.iScience · 2024Article
- 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
- The strand exchange domain of tumor suppressor PALB2 is intrinsically disordered and promotes oligomerization-dependent DNA compaction.bioRxiv : the preprint server for biology · 2024Article
- Article
- The Prothrombin-Prothrombinase Interaction.Sub-cellular biochemistry · 2024Review
- Structural analyses of βJournal of thrombosis and haemostasis : JTH · 2023Article
- Cryo-EM structures of coagulation factors.Research and practice in thrombosis and haemostasis · 2022Review
- Article
- 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
- Discovery and characterization of 2 novel subpopulations of aPS/PT antibodies in patients at high risk of thrombosis.Blood advances · 2019Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The coagulation factor prothrombin has a complex spatial organization of its modular assembly that comprises the N-terminal Gla domain, kringle-1, kringle-2, and the C-terminal protease domain connected by three intervening linkers. Here we use single molecule Förster resonance energy transfer to access the conformational landscape of prothrombin in solution and uncover structural features of functional significance that extend recent x-ray crystallographic analysis. Prothrombin exists in equilibrium between two alternative conformations, open and closed. The closed conformation predominates (70%) and features an unanticipated intramolecular collapse of Tyr(93) in kringle-1 onto Trp(547) in the protease domain that obliterates access to the active site and protects the zymogen from autoproteolytic conversion to thrombin. The open conformation (30%) is more susceptible to chymotrypsin digestion and autoactivation, and features a shape consistent with recent x-ray crystal structures. Small angle x-ray scattering measurements of prothrombin wild type stabilized 70% in the closed conformation and of the mutant Y93A stabilized 80% in the open conformation directly document two envelopes that differ 50 Å in length. These findings reveal important new details on the conformational plasticity of prothrombin in solution and the drastic structural difference between its alternative conformations. Prothrombin uses the intramolecular collapse of kringle-1 onto the active site in the closed form to prevent autoactivation. The open-closed equilibrium also defines a new structural framework for the mechanism of activation of prothrombin by prothrombinase.
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Registered trials
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.