Structural plasticity of SARS-CoV-2 3CL Mpro active site cavity revealed by room temperature X-ray crystallography.
Daniel W KnellerGwyndalyn PhillipsHugh Michael O'NeillRobert JedrzejczakLucy StolsPaul LanganAndrzej JoachimiakLeighton CoatesAndrey Y KovalevskyPublished in: Nature communications (2020)
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.
Keyphrases
- sars cov
- room temperature
- molecular docking
- respiratory syndrome coronavirus
- ionic liquid
- high resolution
- public health
- molecular dynamics simulations
- healthcare
- health information
- mental health
- dual energy
- coronavirus disease
- crystal structure
- mass spectrometry
- magnetic resonance imaging
- risk assessment
- clinical evaluation