| Structural highlights
Publication Abstract from PubMed
The antineoplastic drug carmofur is shown to inhibit the SARS-CoV-2 main protease (M(pro)). Here, the X-ray crystal structure of M(pro) 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 (EC50 = 24.30 muM) and is a promising lead compound to develop new antiviral treatment for COVID-19.
Structural basis for the inhibition of SARS-CoV-2 main protease by antineoplastic drug carmofur.,Jin Z, Zhao Y, Sun Y, Zhang B, Wang H, Wu Y, Zhu Y, Zhu C, Hu T, Du X, Duan Y, Yu J, Yang X, Yang X, Yang K, Liu X, Guddat LW, Xiao G, Zhang L, Yang H, Rao Z Nat Struct Mol Biol. 2020 May 7. pii: 10.1038/s41594-020-0440-6. doi:, 10.1038/s41594-020-0440-6. PMID:32382072[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Jin Z, Zhao Y, Sun Y, Zhang B, Wang H, Wu Y, Zhu Y, Zhu C, Hu T, Du X, Duan Y, Yu J, Yang X, Yang X, Yang K, Liu X, Guddat LW, Xiao G, Zhang L, Yang H, Rao Z. Structural basis for the inhibition of SARS-CoV-2 main protease by antineoplastic drug carmofur. Nat Struct Mol Biol. 2020 May 7. pii: 10.1038/s41594-020-0440-6. doi:, 10.1038/s41594-020-0440-6. PMID:32382072 doi:http://dx.doi.org/10.1038/s41594-020-0440-6
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