Structural Basis for the Inhibition of SARS-CoV-2 M^pro D48N Mutant by Shikonin and PF-07321332.

ABSTRACT: Preventing the spread of SARS-CoV-2 and its variants is crucial in the fight against COVID-19. Inhibition of the main protease (M^pro) of SARS-CoV-2 is the key to disrupting viral replication, making M^pro a promising target for therapy. PF-07321332 and shikonin have been identified as effective broad-spectrum inhibitors of SARS-CoV-2 M^pro. The crystal structures of SARS-CoV-2 M^pro bound to PF-07321332 and shikonin have been resolved in previous studies. However, the exact mechanism regarding how SARS-CoV-2 M^pro mutants impact their binding modes largely remains to be investigated. In this study, we expressed a SARS-CoV-2 M^pro mutant, carrying the D48N substitution, representing a class of mutations located near the active sit

SUBMITTER: Zhao Z 

PROVIDER: S-EPMC10818409 | biostudies-literature | 2023 Dec

REPOSITORIES: biostudies-literature