Allosteric Regulation of 3CL Protease of SARS-CoV-2 and SARS-CoV Observed in the Crystal Structure Ensemble.

ABSTRACT: The 3C-like protease (3CL^pro) of SARS-CoV-2 is a potential therapeutic target for COVID-19. Importantly, it has an abundance of structural information solved as a complex with various drug candidate compounds. Collecting these crystal structures (83 Protein Data Bank (PDB) entries) together with those of the highly homologous 3CL^pro of SARS-CoV (101 PDB entries), we constructed the crystal structure ensemble of 3CL^pro to analyze the dynamic regulation of its catalytic function. The structural dynamics of the 3CL^pro dimer observed in the ensemble were characterized by the motions of four separate loops (the C-loop, E-loop, H-loop, and Linker) and the C-terminal domain III on the rigid core of the chymotrypsin fold. Among the four moving loops, the

SUBMITTER: Kidera A 

PROVIDER: S-EPMC8550881 | biostudies-literature | 2021 Dec

REPOSITORIES: biostudies-literature