ArticleNature communications2023
The H163A mutation unravels an oxidized conformation of the SARS-CoV-2 main protease.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 12 citations in OpenAlex.
- The C117D oxidation mimic reveals the monomeric structure of SARS-CoV-2 main protease.Protein science : a publication of the Protein Society · 2026Article
- From vibrations to function: Spectroscopic detection and quantification of π-π stacking in drug-responsive protein complexes.Science advances · 2026Article
- Next-generation inhibitors of SARS-CoV-2 MNature communications · 2026Article
- A SARS-CoV-2 MNature communications · 2025Article
- SARS-CoV-2 MNature communications · 2024Article
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
The main protease of SARS-CoV-2 (Mpro) is an important target for developing COVID-19 therapeutics. Recent work has highlighted Mpro's susceptibility to undergo redox-associated conformational changes in response to cellular and immune-system-induced oxidation. Despite structural evidence indicating large-scale rearrangements upon oxidation, the mechanisms of conformational change and its functional consequences are poorly understood. Here, we present the crystal structure of an Mpro point mutant (H163A) that shows an oxidized conformation with the catalytic cysteine in a disulfide bond. We hypothesize that Mpro adopts this conformation under oxidative stress to protect against over-oxidation. Our metadynamics simulations illustrate a potential mechanism by which H163 modulates this transition and suggest that this equilibrium exists in the wild type enzyme. We show that other point mutations also significantly shift the equilibrium towards this state by altering conformational free energies. Unique avenues of SARS-CoV-2 research can be explored by understanding how H163 modulates this equilibrium.
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