期刊
NATURE COMMUNICATIONS
卷 11, 期 1, 页码 -出版社
NATURE PORTFOLIO
DOI: 10.1038/s41467-020-16954-7
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资金
- Laboratory Directed Research and Development Program at Oak Ridge National Laboratory (ORNL)
- Scientific User Facilities Division, Office of Basic Energy Sciences, U.S. Department of Energy
- National Institute of Allergy and Infectious Diseases, National Institutes of Health, Department of Health and Human Services [HHSN272201700060C]
- NSF [2029943]
- Office of Biological and Environmental Research
- Div Of Biological Infrastructure
- Direct For Biological Sciences [2029943] Funding Source: National Science Foundation
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 nearphysiological 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.
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