ArticleProceedings of the National Academy of Sciences of the United States of America2010
Crystal structure of prethrombin-1.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 42 citations in OpenAlex.
- Molecular mechanism of cleavage at R271 during prothrombin activation revealed by cryo-EM.Blood · 2026Article
- Reversible High-Affinity Binding of Coagulation Factor Xa to Zeolites Induces Accelerated Blood Coagulation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Quantifying In Situ Structural Stabilities of Human Blood Plasma Proteins Using a Novel Iodination Protein Stability Assay.Journal of proteome research · 2022Article
- Exosite Binding in Thrombin: A Global Structural/Dynamic Overview of Complexes with Aptamers and Other Ligands.International journal of molecular sciences · 2021Review
- Mechanisms of ligand binding.Biophysics reviews · 2020Review
- Probing prothrombin structure by limited proteolysis.Scientific reports · 2019Article
- Identification and characterization of a factor Va-binding site on human prothrombin fragment 2.Scientific reports · 2019Article
- Interplay between conformational selection and zymogen activation.Scientific reports · 2018Article
- Structure of prothrombin in the closed form reveals new details on the mechanism of activation.Scientific reports · 2018Article
- Structural Architecture of Prothrombin in Solution Revealed by Single Molecule Spectroscopy.The Journal of biological chemistry · 2016Article
- The Fragment 1 Region of Prothrombin Facilitates the Favored Binding of Fragment 12 to Zymogen and Enforces Zymogen-like Character in the Proteinase.The Journal of biological chemistry · 2016Article
- Structural transitions during prothrombin activation: On the importance of fragment 2.Biochimie · 2016Article
- The linker connecting the two kringles plays a key role in prothrombin activation.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Histone H4 promotes prothrombin autoactivation.The Journal of biological chemistry · 2013Article
- Article
- Crystal structure of prothrombin reveals conformational flexibility and mechanism of activation.The Journal of biological chemistry · 2013Article
- Autoactivation of thrombin precursors.The Journal of biological chemistry · 2013Article
- Effect of zymogen domains and active site occupation on activation of prothrombin by von Willebrand factor-binding protein.The Journal of biological chemistry · 2012Article
- Significant reduction in errors associated with nonbonded contacts in protein crystal structures: automated all-atom refinement with PrimeX.Acta crystallographica. Section D, Biological crystallography · 2012Article
- Conformational selection in trypsin-like proteases.Current opinion in structural biology · 2012Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Prothrombin is the zymogen precursor of the clotting enzyme thrombin, which is generated by two sequential cleavages at R271 and R320 by the prothrombinase complex. The structure of prothrombin is currently unknown. Prethrombin-1 differs from prothrombin for the absence of 155 residues in the N-terminal domain and is composed of a single polypeptide chain containing fragment 2 (residues 156-271), A chain (residues 272-320), and B chain (residues 321-579). The X-ray crystal structure of prethrombin-1 solved at 2.2-Å resolution shows an overall conformation significantly different (rmsd = 3.6 Å) from that of its active form meizothrombin desF1 carrying a cleavage at R320. Fragment 2 is rotated around the y axis by 29° and makes only few contacts with the B chain. In the B chain, the oxyanion hole is disrupted due to absence of the I16-D194 ion pair and the Na(+) binding site and adjacent primary specificity pocket are highly perturbed. A remarkable feature of the structure is that the autolysis loop assumes a helical conformation enabling W148 and W215, located 17 Å apart in meizothrombin desF1, to come within 3.3 Å of each other and completely occlude access to the active site. These findings suggest that the zymogen form of thrombin possesses conformational plasticity comparable to that of the mature enzyme and have significant implications for the mechanism of prothrombin activation and the zymogen → protease conversion in trypsin-like proteases.
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