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

Kneller, Daniel W.; Phillips, G.N.; O’Neill, Hugh; Jedrzejczak, R.; Stols, Lucy; Langan, Paul; Joachimiak, A.; Coates, Leighton; Kovalevsky, Andrey

doi:10.1038/s41467-020-16954-7

articleNature CommunicationsJun 24, 2020GOLD OA

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

DWDaniel W. Kneller GPG.N. Phillips HOHugh O’Neill RJR. Jedrzejczak LSLucy Stols

Oak Ridge National Laboratory · Argonne National Laboratory · +2 more institutions

PubMed

Indexed incrossrefdoajpubmed

Abstract

Abstract The COVID-19 disease caused by the SARS-CoV-2 coronavirus has become a pandemic health crisis. An attractive target for antiviral inhibitors is the main protease 3CL M pro due to its essential role in processing the polyproteins translated from viral RNA. Here we report the room temperature X-ray structure of unliganded SARS-CoV-2 3CL M pro , revealing the ligand-free structure of the active site and the conformation of the catalytic site cavity at near-physiological temperature. Comparison with previously reported low-temperature ligand-free and inhibitor-bound structures suggest that the room temperature structure may provide more relevant information at physiological temperatures for aiding in…

Citation impact

494

total citations

FWCI: 9.60
Percentile: 100%
References: 44

Citations per year

Authors

9

Topics & keywords

Topics

Keywords

Polyproteins
Active site
Coronavirus disease 2019 (COVID-19)
Docking (animal)
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2)
Ligand (biochemistry)
Coronavirus
Crystallography

UN Sustainable Development Goals

Good health and well-being

No related works found for this paper.