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10.1038/s41467-020-16954-7

http://scihub22266oqcxt.onion/10.1038/s41467-020-16954-7
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32581217!7314768!32581217
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suck abstract from ncbi


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pmid32581217      Nat+Commun 2020 ; 11 (1): 3202
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  • Structural plasticity of SARS-CoV-2 3CL M(pro) active site cavity revealed by room temperature X-ray crystallography #MMPMID32581217
  • Kneller DW; Phillips G; O'Neill HM; Jedrzejczak R; Stols L; Langan P; Joachimiak A; Coates L; Kovalevsky A
  • Nat Commun 2020[Jun]; 11 (1): 3202 PMID32581217show ga
  • 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 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.
  • |Betacoronavirus/*enzymology[MESH]
  • |Catalytic Domain[MESH]
  • |Coronavirus 3C Proteases[MESH]
  • |Crystallography, X-Ray[MESH]
  • |Cysteine Endopeptidases/*chemistry/metabolism[MESH]
  • |Cysteine Proteinase Inhibitors/metabolism[MESH]
  • |Ligands[MESH]
  • |Models, Molecular[MESH]
  • |Molecular Dynamics Simulation[MESH]
  • |Protein Binding[MESH]
  • |Protein Conformation[MESH]
  • |Protein Domains[MESH]
  • |Protein Structure, Secondary[MESH]
  • |SARS-CoV-2[MESH]
  • |Temperature[MESH]


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