The P132H mutation in the main protease of Omicron SARS-CoV-2 decreases thermal stability without compromising catalysis or small-molecule drug inhibition.

Sacco, Michael Dominic; Hu, Yanmei; Gongora, Maura Verenice; Meilleur, Flora; Kemp, Michael Trent; Zhang, Xiujun; Wang, Jun; Chen, Yu

Sacco, Michael Dominic; Hu, Yanmei; Gongora, Maura Verenice; Meilleur, Flora; Kemp, Michael Trent; Zhang, Xiujun; Wang, Jun; Chen, Yu.

Sacco MD; Department of Molecular Medicine, Morsani College of Medicine, University of South Florida, Tampa, FL, USA.
Hu Y; Department of Medicinal Chemistry, Ernest Mario School of Pharmacy, Rutgers, the State University of New Jersey, Piscataway, NJ, USA.
Gongora MV; Department of Molecular Medicine, Morsani College of Medicine, University of South Florida, Tampa, FL, USA.
Meilleur F; Department of Molecular and Structural Biochemistry, North Carolina State University, Raleigh, NC, USA.
Kemp MT; Neutron Scattering Division, Oak Ridge National Laboratory, Oak Ridge, TN, USA.
Zhang X; Department of Molecular Medicine, Morsani College of Medicine, University of South Florida, Tampa, FL, USA.
Wang J; Department of Molecular Medicine, Morsani College of Medicine, University of South Florida, Tampa, FL, USA.
Chen Y; Department of Medicinal Chemistry, Ernest Mario School of Pharmacy, Rutgers, the State University of New Jersey, Piscataway, NJ, USA. junwang@pharmacy.rutgers.edu.

Cell Res ; 32(5): 498-500, 2022 05.

Article in English | MEDLINE | ID: covidwho-1747244

Subject(s)

COVID-19; SARS-CoV-2; Catalysis; Humans; Mutation/genetics; Peptide Hydrolases

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Full text: Available Collection: International databases Database: MEDLINE Main subject: SARS-CoV-2 / COVID-19 Topics: Variants Limits: Humans Language: English Journal: Cell Res Year: 2022 Document Type: Article Affiliation country: S41422-022-00640-y

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