ArticleJournal of thrombosis and haemostasis : JTH2024
Conformation of factor Xa in solution revealed by single-molecule spectroscopy.
Article in Journal of thrombosis and haemostasis : JTH, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Molecular mechanism of cleavage at R271 during prothrombin activation revealed by cryo-EM.Blood · 2026Article
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2 authors.
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Abstract
backgroundAll current X-ray structures of factor (F)Xa are devoid of the γ-carboxyglutamate (Gla) domain and fail to reveal the overall conformation of the free protein. The recent cryogenic electron microscopy (cryo-EM) structure of FXa in the prothrombinase complex is the only structure of full-length FXa and shows that the Gla domain is positioned at an angle relative to the epidermal growth factor 1 domain.
objectivesEstablish if the curved conformation of FXa revealed by cryo-EM is also present in solution.
methodsThe conformation of FXa in solution was studied by single-molecule Förster resonance energy transfer.
resultsThe conformation of full-length FXa in solution is resolved for the first time. The conformation is curved and extremely sensitive to Ca
conclusionMeasurements by single-molecule Förster resonance energy transfer reveal that FXa has a curved conformation in solution, free or bound to physiologic ligands, and validate the recent cryo-EM structures of prothrombinase. The drastic conformational changes observed in the absence of Ca
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