Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 27, Issue 6, Pages 529-+Publisher
NATURE PORTFOLIO
DOI: 10.1038/s41594-020-0440-6
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Funding
- National Key R&D Program of China [2017YFC0840300, 2020YFA0707500]
- Project of International Cooperation and Exchanges NSFC [81520108019]
- Science and Technology Commission of Shanghai Municipality [20431900200]
- Department of Science and Technology of Guangxi Zhuang Autonomous Region [2020AB40007]
- Natural Science Foundation of China [31970165]
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A crystal structure of SARS-CoV-2 with inhibitor carmofur reveals the mechanism of action of this compound and opens the way to develop more potent drugs. 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 mu M) and is a promising lead compound to develop new antiviral treatment for COVID-19.
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