Selected article for: "available protein and betweenness centrality"

Author: Griffin, Jeddidiah W.D.
Title: SARS-CoV and SARS-CoV-2 main protease residue interaction networks change when bound to inhibitor N3
  • Cord-id: 3f6abahf
  • Document date: 2020_7_10
  • ID: 3f6abahf
    Snippet: 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 are available in the Protein Data Bank of the main proteases of SARS-CoV and SARS-CoV-2 with and without inhibitor N3. Comparing these structures revealed residue interaction network changes associated
    Document: 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 are available in the Protein Data Bank of the main proteases of SARS-CoV and SARS-CoV-2 with and without inhibitor N3. 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.

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