Crystallographic structure of wild-type SARS-CoV-2 main protease acyl-enzyme intermediate with physiological C-terminal autoprocessing site

The SARS-CoV-2 main protease (Mpro) is one of two cysteine proteases essential for viral replication. Here, the authors determine the crystal structure of an Mpro acyl intermediate with its native C-terminal autocleavage sequence and the structure of a product bound active site mutant (C145A), which...

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Autores principales:	Jaeyong Lee, Liam J. Worrall, Marija Vuckovic, Federico I. Rosell, Francesco Gentile, Anh-Tien Ton, Nathanael A. Caveney, Fuqiang Ban, Artem Cherkasov, Mark Paetzel, Natalie C. J. Strynadka
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/79fa01c0d7f04a9ab66a27ea9f850fb5
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spelling	oai:doaj.org-article:79fa01c0d7f04a9ab66a27ea9f850fb52021-12-02T15:39:22ZCrystallographic structure of wild-type SARS-CoV-2 main protease acyl-enzyme intermediate with physiological C-terminal autoprocessing site10.1038/s41467-020-19662-42041-1723https://doaj.org/article/79fa01c0d7f04a9ab66a27ea9f850fb52020-11-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-19662-4https://doaj.org/toc/2041-1723The SARS-CoV-2 main protease (Mpro) is one of two cysteine proteases essential for viral replication. Here, the authors determine the crystal structure of an Mpro acyl intermediate with its native C-terminal autocleavage sequence and the structure of a product bound active site mutant (C145A), which are of interest for antiviral drug development.Jaeyong LeeLiam J. WorrallMarija VuckovicFederico I. RosellFrancesco GentileAnh-Tien TonNathanael A. CaveneyFuqiang BanArtem CherkasovMark PaetzelNatalie C. J. StrynadkaNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-9 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Jaeyong Lee Liam J. Worrall Marija Vuckovic Federico I. Rosell Francesco Gentile Anh-Tien Ton Nathanael A. Caveney Fuqiang Ban Artem Cherkasov Mark Paetzel Natalie C. J. Strynadka Crystallographic structure of wild-type SARS-CoV-2 main protease acyl-enzyme intermediate with physiological C-terminal autoprocessing site
description	The SARS-CoV-2 main protease (Mpro) is one of two cysteine proteases essential for viral replication. Here, the authors determine the crystal structure of an Mpro acyl intermediate with its native C-terminal autocleavage sequence and the structure of a product bound active site mutant (C145A), which are of interest for antiviral drug development.
format	article
author	Jaeyong Lee Liam J. Worrall Marija Vuckovic Federico I. Rosell Francesco Gentile Anh-Tien Ton Nathanael A. Caveney Fuqiang Ban Artem Cherkasov Mark Paetzel Natalie C. J. Strynadka
author_facet	Jaeyong Lee Liam J. Worrall Marija Vuckovic Federico I. Rosell Francesco Gentile Anh-Tien Ton Nathanael A. Caveney Fuqiang Ban Artem Cherkasov Mark Paetzel Natalie C. J. Strynadka
author_sort	Jaeyong Lee
title	Crystallographic structure of wild-type SARS-CoV-2 main protease acyl-enzyme intermediate with physiological C-terminal autoprocessing site
title_short	Crystallographic structure of wild-type SARS-CoV-2 main protease acyl-enzyme intermediate with physiological C-terminal autoprocessing site
title_full	Crystallographic structure of wild-type SARS-CoV-2 main protease acyl-enzyme intermediate with physiological C-terminal autoprocessing site
title_fullStr	Crystallographic structure of wild-type SARS-CoV-2 main protease acyl-enzyme intermediate with physiological C-terminal autoprocessing site
title_full_unstemmed	Crystallographic structure of wild-type SARS-CoV-2 main protease acyl-enzyme intermediate with physiological C-terminal autoprocessing site
title_sort	crystallographic structure of wild-type sars-cov-2 main protease acyl-enzyme intermediate with physiological c-terminal autoprocessing site
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/79fa01c0d7f04a9ab66a27ea9f850fb5
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Crystallographic structure of wild-type SARS-CoV-2 main protease acyl-enzyme intermediate with physiological C-terminal autoprocessing site

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