Structural plasticity of SARS-CoV-2 3CL Mpro active site cavity revealed by room temperature X-ray crystallography
Data
2020-06-24Autor
Kneller, Daniel W.
Phillips, Gwyndalyn
O’Neill, Hugh M.
Jedrzejczak, Robert
Stols, Lucy
Langan, Paul
Joachimiak, Andrzej
Coates, Leighton
Kovalevsky, Andrey
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Resumo em língua estrangeira
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.
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SARS-CoV-2Link para o recurso
https://www.nature.com/articles/s41467-020-16954-7Collections
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