Unmasking the Conformational Stability and Inhibitor Binding to SARS-CoV-2 Main Protease Active Site Mutants and Miniprecursor

We recently demonstrated that inhibitor binding reorganizes the oxyanion loop of a monomeric catalytic domain of SARS CoV-2 main protease (MPro) from an unwound (E) to a wound (active, E*) conformation, independent of dimerization. Here we assess the effect of the flanking N-terminal residues, to im...

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Detalles Bibliográficos
Autores principales: Kovalevsky, Andrey, Coates, Leighton, Kneller, Daniel W., Ghirlando, Rodolfo, Aniana, Annie, Nashed, Nashaat T., Louis, John M.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2022
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9628131/
https://www.ncbi.nlm.nih.gov/pubmed/36334779
http://dx.doi.org/10.1016/j.jmb.2022.167876

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9628131/
https://www.ncbi.nlm.nih.gov/pubmed/36334779
http://dx.doi.org/10.1016/j.jmb.2022.167876

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