Structural plasticity of SARS-CoV-2 3CL M<sup>pro</sup> active site cavity revealed by room temperature X-ray crystallography.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 32581217.
- Also identified by DOI 10.1038/s41467-020-16954-7 and PMC identifier 7314768.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
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<sup>pro</sup> 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<sup>pro</sup>, 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.
Medical subject headings
- Betacoronavirus
- Cysteine Endopeptidases
- Viral Nonstructural Proteins