Structural plasticity of SARS-CoV-2 3CL Mpro active site cavity revealed by room temperature X-ray crystallography
Nature Communications2020Vol. 11(1), pp. 3202–3202
Citations Over TimeTop 10% of 2020 papers
Daniel W. Kneller, G.N. Phillips, Hugh O’Neill, R. Jedrzejczak, Lucy Stols, Paul Langan, A. Joachimiak, Leighton Coates, Andrey Kovalevsky
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 Mpro 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 Mpro, 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 molecular docking studies.
Related Papers
- → Interflap Distances in HIV-1 Protease Determined by Pulsed EPR Measurements(2007)57 cited
- → HIV protease: Enzyme function and drug resistance(2000)49 cited
- → Analyzing 3D structures of the SARS-CoV-2 main protease reveals structural features of ligand binding for COVID-19 drug discovery(2023)6 cited
- → Methodology and Problems of Protein‐Ligand Docking: Case Study of Dihydroorotate Dehydrogenase, Thymidine Kinase, and Phosphodiesterase 4(2002)29 cited
- → Effect of two novel inhibitors of the human immunodeficiency virus protease on the maturation of the HIV gag and gag-pol polyproteins(1990)29 cited