X-ray crystallographic characterization of the SARS-CoV-2 main protease polyprotein cleavage sites essential for viral processing and maturation
The SARS-CoV-2 protease Mpro is essential for viral replication. Here, the authors have determined the structures of Mpro in complex with 10 of the 11 viral cleavage sequences including a covalent acyl-enzyme intermediate, providing mechanistic and structural insights for antiviral development.
| Main Authors: | , , , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2022-09-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-022-32854-4 |
| _version_ | 1798032052872806400 |
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| author | Jaeyong Lee Calem Kenward Liam J. Worrall Marija Vuckovic Francesco Gentile Anh-Tien Ton Myles Ng Artem Cherkasov Natalie C. J. Strynadka Mark Paetzel |
| author_facet | Jaeyong Lee Calem Kenward Liam J. Worrall Marija Vuckovic Francesco Gentile Anh-Tien Ton Myles Ng Artem Cherkasov Natalie C. J. Strynadka Mark Paetzel |
| author_sort | Jaeyong Lee |
| collection | DOAJ |
| description | The SARS-CoV-2 protease Mpro is essential for viral replication. Here, the authors have determined the structures of Mpro in complex with 10 of the 11 viral cleavage sequences including a covalent acyl-enzyme intermediate, providing mechanistic and structural insights for antiviral development. |
| first_indexed | 2024-04-11T20:07:45Z |
| format | Article |
| id | doaj.art-1bd44754c8b142a281ac22dd1d9222a1 |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-04-11T20:07:45Z |
| publishDate | 2022-09-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-1bd44754c8b142a281ac22dd1d9222a12022-12-22T04:05:16ZengNature PortfolioNature Communications2041-17232022-09-0113111310.1038/s41467-022-32854-4X-ray crystallographic characterization of the SARS-CoV-2 main protease polyprotein cleavage sites essential for viral processing and maturationJaeyong Lee0Calem Kenward1Liam J. Worrall2Marija Vuckovic3Francesco Gentile4Anh-Tien Ton5Myles Ng6Artem Cherkasov7Natalie C. J. Strynadka8Mark Paetzel9Department of Biochemistry and Molecular Biology and Centre for Blood Research, The University of British ColumbiaDepartment of Biochemistry and Molecular Biology and Centre for Blood Research, The University of British ColumbiaDepartment of Biochemistry and Molecular Biology and Centre for Blood Research, The University of British ColumbiaDepartment of Biochemistry and Molecular Biology and Centre for Blood Research, The University of British ColumbiaVancouver Prostate Centre, The University of British ColumbiaVancouver Prostate Centre, The University of British ColumbiaDepartment of Biochemistry and Molecular Biology and Centre for Blood Research, The University of British ColumbiaVancouver Prostate Centre, The University of British ColumbiaDepartment of Biochemistry and Molecular Biology and Centre for Blood Research, The University of British ColumbiaDepartment of Molecular Biology and Biochemistry, Simon Fraser UniversityThe SARS-CoV-2 protease Mpro is essential for viral replication. Here, the authors have determined the structures of Mpro in complex with 10 of the 11 viral cleavage sequences including a covalent acyl-enzyme intermediate, providing mechanistic and structural insights for antiviral development.https://doi.org/10.1038/s41467-022-32854-4 |
| spellingShingle | Jaeyong Lee Calem Kenward Liam J. Worrall Marija Vuckovic Francesco Gentile Anh-Tien Ton Myles Ng Artem Cherkasov Natalie C. J. Strynadka Mark Paetzel X-ray crystallographic characterization of the SARS-CoV-2 main protease polyprotein cleavage sites essential for viral processing and maturation Nature Communications |
| title | X-ray crystallographic characterization of the SARS-CoV-2 main protease polyprotein cleavage sites essential for viral processing and maturation |
| title_full | X-ray crystallographic characterization of the SARS-CoV-2 main protease polyprotein cleavage sites essential for viral processing and maturation |
| title_fullStr | X-ray crystallographic characterization of the SARS-CoV-2 main protease polyprotein cleavage sites essential for viral processing and maturation |
| title_full_unstemmed | X-ray crystallographic characterization of the SARS-CoV-2 main protease polyprotein cleavage sites essential for viral processing and maturation |
| title_short | X-ray crystallographic characterization of the SARS-CoV-2 main protease polyprotein cleavage sites essential for viral processing and maturation |
| title_sort | x ray crystallographic characterization of the sars cov 2 main protease polyprotein cleavage sites essential for viral processing and maturation |
| url | https://doi.org/10.1038/s41467-022-32854-4 |
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