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10.1016/j.jsb.2020.107575

http://scihub22266oqcxt.onion/10.1016/j.jsb.2020.107575
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suck abstract from ncbi


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pmid32653646      J+Struct+Biol 2020 ; 211 (3): 107575
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  • SARS-CoV and SARS-CoV-2 main protease residue interaction networks change when bound to inhibitor N3 #MMPMID32653646
  • Griffin JWD
  • J Struct Biol 2020[Sep]; 211 (3): 107575 PMID32653646show ga
  • COVID-19 is a respiratory disease caused by the coronavirus SARS-CoV-2. SARS-CoV-2 has many similarities with SARS-CoV. Both viruses rely on a protease called the main protease, or M(pro), for replication. Therefore, inhibiting M(pro) may be a successful strategy for treating COVID-19. Structures of the main proteases of SARS-CoV and SARS-CoV-2 with and without inhibitor N3 are available in the Protein Data Bank. Comparing these structures revealed residue interaction network changes associated with N3 inhibition. Comparing network clustering with and without inhibitor N3 identified the formation of a cluster of residues 17, 18, 30-33, 70, 95, 98, 103, 117, 122, and 177 as a network change in both viral proteases when bound to inhibitor N3. Betweenness and stress centrality differences as well as differences in bond energies and relative B-factors when comparing free M(pro) to inhibitor-bound M(pro) identified residues 131, 175, 182, and 185 as possibly conformationally relevant when bound to the inhibitor N3. Taken together, these results provide insight into conformational changes of betacoronavirus M(pro)s when bound to an inhibitor.
  • |Antiviral Agents/*pharmacology[MESH]
  • |Betacoronavirus/*enzymology[MESH]
  • |COVID-19[MESH]
  • |COVID-19 Drug Treatment[MESH]
  • |Catalytic Domain[MESH]
  • |Cluster Analysis[MESH]
  • |Coronavirus 3C Proteases[MESH]
  • |Coronavirus Infections/drug therapy[MESH]
  • |Cysteine Endopeptidases[MESH]
  • |Drug Design[MESH]
  • |Enzyme Inhibitors/*pharmacology[MESH]
  • |Humans[MESH]
  • |Pandemics[MESH]
  • |Pneumonia, Viral/drug therapy[MESH]
  • |Polyproteins[MESH]
  • |Protein Binding[MESH]
  • |SARS-CoV-2[MESH]
  • |Severe acute respiratory syndrome-related coronavirus/*enzymology[MESH]
  • |Viral Nonstructural Proteins/*antagonists & inhibitors[MESH]


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