Cryo‐EM structures of coagulation factors
Abstract A State of the Art lecture titled “Cryo‐EM structures of coagulation factors” was presented at the ISTH Congress in 2022. Cryogenic electron microscopy (cryo‐EM) is a revolutionary technique capable of solving the structure of high molecular weight proteins and their complexes, unlike nucle...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
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Elsevier
2022-10-01
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| Series: | Research and Practice in Thrombosis and Haemostasis |
| Subjects: | |
| Online Access: | https://doi.org/10.1002/rth2.12830 |
| _version_ | 1797710313702817792 |
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| author | Enrico Di Cera Bassem M. Mohammed Leslie A. Pelc Bosko M. Stojanovski |
| author_facet | Enrico Di Cera Bassem M. Mohammed Leslie A. Pelc Bosko M. Stojanovski |
| author_sort | Enrico Di Cera |
| collection | DOAJ |
| description | Abstract A State of the Art lecture titled “Cryo‐EM structures of coagulation factors” was presented at the ISTH Congress in 2022. Cryogenic electron microscopy (cryo‐EM) is a revolutionary technique capable of solving the structure of high molecular weight proteins and their complexes, unlike nuclear magnetic resonance (NMR), and under conditions not biased by crystal contacts, unlike X‐ray crystallography. These features are particularly relevant to the analysis of coagulation factors that are too big for NMR and often recalcitrant to X‐ray investigation. Using cryo‐EM, we have solved the structures of coagulation factors V and Va, prothrombinase on nanodiscs, and the prothrombin‐prothrombinase complex. These structures have advanced basic knowledge in the field of thrombosis and hemostasis, especially on the function of factor V and the molecular mechanism for prothrombin activation, and set the stage for exciting new lines of investigation. Finally, we summarize relevant new data on this topic presented during the 2022 ISTH Congress. |
| first_indexed | 2024-03-12T06:50:22Z |
| format | Article |
| id | doaj.art-9bf0407086324aaf8c9481a3d6fa9262 |
| institution | Directory Open Access Journal |
| issn | 2475-0379 |
| language | English |
| last_indexed | 2024-03-12T06:50:22Z |
| publishDate | 2022-10-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Research and Practice in Thrombosis and Haemostasis |
| spelling | doaj.art-9bf0407086324aaf8c9481a3d6fa92622023-09-03T00:20:10ZengElsevierResearch and Practice in Thrombosis and Haemostasis2475-03792022-10-0167n/an/a10.1002/rth2.12830Cryo‐EM structures of coagulation factorsEnrico Di Cera0Bassem M. Mohammed1Leslie A. Pelc2Bosko M. Stojanovski3Edward A. Doisy Department of Biochemistry and Molecular Biology Saint Louis University School of Medicine St. Louis Missouri USAEdward A. Doisy Department of Biochemistry and Molecular Biology Saint Louis University School of Medicine St. Louis Missouri USAEdward A. Doisy Department of Biochemistry and Molecular Biology Saint Louis University School of Medicine St. Louis Missouri USAEdward A. Doisy Department of Biochemistry and Molecular Biology Saint Louis University School of Medicine St. Louis Missouri USAAbstract A State of the Art lecture titled “Cryo‐EM structures of coagulation factors” was presented at the ISTH Congress in 2022. Cryogenic electron microscopy (cryo‐EM) is a revolutionary technique capable of solving the structure of high molecular weight proteins and their complexes, unlike nuclear magnetic resonance (NMR), and under conditions not biased by crystal contacts, unlike X‐ray crystallography. These features are particularly relevant to the analysis of coagulation factors that are too big for NMR and often recalcitrant to X‐ray investigation. Using cryo‐EM, we have solved the structures of coagulation factors V and Va, prothrombinase on nanodiscs, and the prothrombin‐prothrombinase complex. These structures have advanced basic knowledge in the field of thrombosis and hemostasis, especially on the function of factor V and the molecular mechanism for prothrombin activation, and set the stage for exciting new lines of investigation. Finally, we summarize relevant new data on this topic presented during the 2022 ISTH Congress.https://doi.org/10.1002/rth2.12830blood coagulationfactor Vfactor Vaprothrombinvitamin K‐dependent clotting factors |
| spellingShingle | Enrico Di Cera Bassem M. Mohammed Leslie A. Pelc Bosko M. Stojanovski Cryo‐EM structures of coagulation factors Research and Practice in Thrombosis and Haemostasis blood coagulation factor V factor Va prothrombin vitamin K‐dependent clotting factors |
| title | Cryo‐EM structures of coagulation factors |
| title_full | Cryo‐EM structures of coagulation factors |
| title_fullStr | Cryo‐EM structures of coagulation factors |
| title_full_unstemmed | Cryo‐EM structures of coagulation factors |
| title_short | Cryo‐EM structures of coagulation factors |
| title_sort | cryo em structures of coagulation factors |
| topic | blood coagulation factor V factor Va prothrombin vitamin K‐dependent clotting factors |
| url | https://doi.org/10.1002/rth2.12830 |
| work_keys_str_mv | AT enricodicera cryoemstructuresofcoagulationfactors AT bassemmmohammed cryoemstructuresofcoagulationfactors AT leslieapelc cryoemstructuresofcoagulationfactors AT boskomstojanovski cryoemstructuresofcoagulationfactors |