Contribution of the catalytic dyad of SARS-CoV-2 main protease to binding covalent and noncovalent inhibitors.

Kovalevsky, Andrey; Aniana, Annie; Coates, Leighton; Bonnesen, Peter V; Nashed, Nashaat T; Louis, John M

Kovalevsky, Andrey; Aniana, Annie; Coates, Leighton; Bonnesen, Peter V; Nashed, Nashaat T; Louis, John M.

Affiliation

Kovalevsky A; Neutron Scattering Division, Oak Ridge National Laboratory, Oak Ridge, Tennessee, USA. Electronic address: kovalevskyay@ornl.gov.
Aniana A; Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, DHHS, Bethesda, Maryland, USA.
Coates L; Second Target Station, Oak Ridge National Laboratory, Oak Ridge, Tennessee, USA.
Bonnesen PV; Center for Nanophase Materials Sciences, Oak Ridge National Laboratory, Oak Ridge, Tennessee, USA.
Nashed NT; Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, DHHS, Bethesda, Maryland, USA.
Louis JM; Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, DHHS, Bethesda, Maryland, USA. Electronic address: johnl@niddk.nih.gov.

J Biol Chem ; 299(7): 104886, 2023 07.

Article de En | MEDLINE | ID: mdl-37271339

Sujet(s)
Mots clés

C145A/H41A mutations; SARS-CoV-2 main protease; inhibitor binding thermodynamics; main protease inhibitors; room-temperature X-ray crystallography; thermal stability

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Texte intégral: 1 Collection: 01-internacional Base de données: MEDLINE Sujet principal: Inhibiteurs des protéases des coronavirus / SARS-CoV-2 / COVID-19 Limites: Humans Langue: En Journal: J Biol Chem Année: 2023 Type de document: Article Pays de publication: États-Unis d'Amérique

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