Cargando…
Direct Observation of Protonation State Modulation in SARS-CoV-2 Main Protease upon Inhibitor Binding with Neutron Crystallography
[Image: see text] The main protease (3CL M(pro)) from severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), the virus that causes COVID-19, is an essential enzyme for viral replication with no human counterpart, making it an attractive drug target. To date, no small-molecule clinical drugs a...
Autores principales: | Kneller, Daniel W., Phillips, Gwyndalyn, Weiss, Kevin L., Zhang, Qiu, Coates, Leighton, Kovalevsky, Andrey |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical
Society
2021
|
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8009097/ https://www.ncbi.nlm.nih.gov/pubmed/33755450 http://dx.doi.org/10.1021/acs.jmedchem.1c00058 |
Ejemplares similares
-
Unusual zwitterionic catalytic site of SARS–CoV-2 main protease revealed by neutron crystallography
por: Kneller, Daniel W., et al.
Publicado: (2020) -
Covalent narlaprevir- and boceprevir-derived hybrid inhibitors of SARS-CoV-2 main protease: room-temperature X-ray and neutron crystallography, binding thermodynamics, and antiviral activity
por: Kneller, Daniel, et al.
Publicado: (2022) -
Room-temperature neutron and X-ray data collection of 3CL M(pro) from SARS-CoV-2
por: Kneller, Daniel W., et al.
Publicado: (2020) -
Michaelis-like complex of SARS-CoV-2 main protease visualized by room-temperature X-ray crystallography
por: Kneller, Daniel W., et al.
Publicado: (2021) -
Room-temperature X-ray crystallography reveals the oxidation and reactivity of cysteine residues in SARS-CoV-2 3CL M(pro): insights into enzyme mechanism and drug design
por: Kneller, Daniel W., et al.
Publicado: (2020)