Structural plasticity of SARS-CoV-2 3CL Mpro active site cavity revealed by room temperature X-ray crystallography

The SARS-CoV-2 3CL main protease (3CL Mpro) is a chymotrypsin-like protease that facilitates the production of non-structural proteins, which are essential for viral replication and is therefore of great interest as a drug target. Here, the authors present the 2.30 Å room temperature crystal structu...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Daniel W. Kneller, Gwyndalyn Phillips, Hugh M. O’Neill, Robert Jedrzejczak, Lucy Stols, Paul Langan, Andrzej Joachimiak, Leighton Coates, Andrey Kovalevsky
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/b4c49bbea9c247e4bb006a3c2edf71ae
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:b4c49bbea9c247e4bb006a3c2edf71ae
record_format	dspace
spelling	oai:doaj.org-article:b4c49bbea9c247e4bb006a3c2edf71ae2021-12-02T17:12:24ZStructural plasticity of SARS-CoV-2 3CL Mpro active site cavity revealed by room temperature X-ray crystallography10.1038/s41467-020-16954-72041-1723https://doaj.org/article/b4c49bbea9c247e4bb006a3c2edf71ae2020-06-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-16954-7https://doaj.org/toc/2041-1723The SARS-CoV-2 3CL main protease (3CL Mpro) is a chymotrypsin-like protease that facilitates the production of non-structural proteins, which are essential for viral replication and is therefore of great interest as a drug target. Here, the authors present the 2.30 Å room temperature crystal structure of ligand-free 3CL Mpro and compare it with the earlier determined low-temperature ligand-free and inhibitor-bound crystal structures.Daniel W. KnellerGwyndalyn PhillipsHugh M. O’NeillRobert JedrzejczakLucy StolsPaul LanganAndrzej JoachimiakLeighton CoatesAndrey KovalevskyNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-6 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Daniel W. Kneller Gwyndalyn Phillips Hugh M. O’Neill Robert Jedrzejczak Lucy Stols Paul Langan Andrzej Joachimiak Leighton Coates Andrey Kovalevsky Structural plasticity of SARS-CoV-2 3CL Mpro active site cavity revealed by room temperature X-ray crystallography
description	The SARS-CoV-2 3CL main protease (3CL Mpro) is a chymotrypsin-like protease that facilitates the production of non-structural proteins, which are essential for viral replication and is therefore of great interest as a drug target. Here, the authors present the 2.30 Å room temperature crystal structure of ligand-free 3CL Mpro and compare it with the earlier determined low-temperature ligand-free and inhibitor-bound crystal structures.
format	article
author	Daniel W. Kneller Gwyndalyn Phillips Hugh M. O’Neill Robert Jedrzejczak Lucy Stols Paul Langan Andrzej Joachimiak Leighton Coates Andrey Kovalevsky
author_facet	Daniel W. Kneller Gwyndalyn Phillips Hugh M. O’Neill Robert Jedrzejczak Lucy Stols Paul Langan Andrzej Joachimiak Leighton Coates Andrey Kovalevsky
author_sort	Daniel W. Kneller
title	Structural plasticity of SARS-CoV-2 3CL Mpro active site cavity revealed by room temperature X-ray crystallography
title_short	Structural plasticity of SARS-CoV-2 3CL Mpro active site cavity revealed by room temperature X-ray crystallography
title_full	Structural plasticity of SARS-CoV-2 3CL Mpro active site cavity revealed by room temperature X-ray crystallography
title_fullStr	Structural plasticity of SARS-CoV-2 3CL Mpro active site cavity revealed by room temperature X-ray crystallography
title_full_unstemmed	Structural plasticity of SARS-CoV-2 3CL Mpro active site cavity revealed by room temperature X-ray crystallography
title_sort	structural plasticity of sars-cov-2 3cl mpro active site cavity revealed by room temperature x-ray crystallography
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/b4c49bbea9c247e4bb006a3c2edf71ae
work_keys_str_mv	AT danielwkneller structuralplasticityofsarscov23clmproactivesitecavityrevealedbyroomtemperaturexraycrystallography AT gwyndalynphillips structuralplasticityofsarscov23clmproactivesitecavityrevealedbyroomtemperaturexraycrystallography AT hughmoneill structuralplasticityofsarscov23clmproactivesitecavityrevealedbyroomtemperaturexraycrystallography AT robertjedrzejczak structuralplasticityofsarscov23clmproactivesitecavityrevealedbyroomtemperaturexraycrystallography AT lucystols structuralplasticityofsarscov23clmproactivesitecavityrevealedbyroomtemperaturexraycrystallography AT paullangan structuralplasticityofsarscov23clmproactivesitecavityrevealedbyroomtemperaturexraycrystallography AT andrzejjoachimiak structuralplasticityofsarscov23clmproactivesitecavityrevealedbyroomtemperaturexraycrystallography AT leightoncoates structuralplasticityofsarscov23clmproactivesitecavityrevealedbyroomtemperaturexraycrystallography AT andreykovalevsky structuralplasticityofsarscov23clmproactivesitecavityrevealedbyroomtemperaturexraycrystallography
_version_	1718381400403476480

Structural plasticity of SARS-CoV-2 3CL Mpro active site cavity revealed by room temperature X-ray crystallography

Ejemplares similares