SARS-CoV and SARS-CoV-2 main protease residue interaction networks change when bound to inhibitor N3.

ABSTRACT: 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 centrali

SUBMITTER: Griffin JWD 

PROVIDER: S-EPMC7347504 | biostudies-literature | 2020 Sep

REPOSITORIES: biostudies-literature