Nature structural & molecular biology, 2020-06, Vol.27 (6), p.529
2020
Details
- Autor(en) / Beteiligte
- Titel
- Structural basis for the inhibition of SARS-CoV-2 main protease by antineoplastic drug carmofur
- Ist Teil von
- Nature structural & molecular biology, 2020-06, Vol.27 (6), p.529
- Ort / Verlag
- United States
- Erscheinungsjahr
- 2020
- Link zum Volltext
- Quelle
- MEDLINE
- Beschreibungen/Notizen
- The antineoplastic drug carmofur is shown to inhibit the SARS-CoV-2 main protease (M ). Here, the X-ray crystal structure of M in complex with carmofur reveals that the carbonyl reactive group of carmofur is covalently bound to catalytic Cys145, whereas its fatty acid tail occupies the hydrophobic S2 subsite. Carmofur inhibits viral replication in cells (EC = 24.30 μM) and is a promising lead compound to develop new antiviral treatment for COVID-19.
- Sprache
- Englisch
- Identifikatoren
- eISSN: 1545-9985DOI: 10.1038/s41594-020-0440-6Titel-ID: cdi_pubmed_primary_32382072
- Format
- –
- Schlagworte
- Animals, Betacoronavirus - drug effects, Betacoronavirus - enzymology, Chlorocebus aethiops, Coronavirus 3C Proteases, Coronavirus Infections - virology, COVID-19, Cysteine Endopeptidases - chemistry, Cysteine Endopeptidases - genetics, Cysteine Endopeptidases - metabolism, Fluorouracil - analogs & derivatives, Fluorouracil - chemistry, Fluorouracil - pharmacology, Models, Molecular, Pandemics, Pneumonia, Viral - virology, SARS-CoV-2, Vero Cells, Viral Nonstructural Proteins - antagonists & inhibitors, Viral Nonstructural Proteins - chemistry, Viral Nonstructural Proteins - genetics, Viral Nonstructural Proteins - metabolism