| Literature DB >> 32382072 |
Zhenming Jin1,2, Yao Zhao1, Yuan Sun3, Bing Zhang1, Haofeng Wang1,4, Yan Wu3, Yan Zhu1, Chen Zhu1, Tianyu Hu1, Xiaoyu Du1,2, Yinkai Duan1, Jing Yu1, Xiaobao Yang1, Xiuna Yang1, Kailin Yang5, Xiang Liu6, Luke W Guddat7, Gengfu Xiao3, Leike Zhang8, Haitao Yang9, Zihe Rao1,2,6.
Abstract
The antineoplastic drug carmofur is shown to inhibit the SARS-CoV-2 main protease (Mpro). Here, the X-ray crystal structure of Mpro 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 μM) and is a promising lead compound to develop new antiviral treatment for COVID-19.Entities:
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Year: 2020 PMID： 32382072 DOI： 10.1038/s41594-020-0440-6
Source DB: PubMed Journal: Nat Struct Mol Biol ISSN： 1545-9985 Impact factor: 15.369