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Article

Visualizing the Active Site Oxyanion Loop Transition Upon Ensitrelvir Binding and Transient Dimerization of SARS-CoV-2 Main Protease.

Journal of molecular biology - 1 Jul 2024

Kovalevsky Andrey, Aniana Annie, Coates Leighton, Ghirlando Rodolfo, Nashed Nashaat T, Louis John M

Abstract excerpt

N-terminal autoprocessing from its polyprotein precursor enables creating the mature-like stable dimer interface of SARS-CoV-2 main protease (MPro), concomitant with the active site oxyanion loop equilibrium transitioning to the active conformation (E*) and onset of catalytic activity. Through mutagenesis of critical interface residues and evaluating noncovalent inhibitor (ensitrelvir, ESV) facilitated...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 38762033
DOI: 10.1016/j.jmb.2024.168616
PMCID: PMC11182712

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