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Structural basis for the inhibition of SARS-CoV-2 main protease by antineoplastic drug Carmofur

By Zhenming Jin, Suwen Zhao, Yuan Sun, Bing Zhang, Haofeng Wang, Yan Wu, Yan Zhu, Chen Zhu, Tianyu Hu, Xiaoyu Du, Yinkai Duan, Jing Yu, Xiaobao Yang, Xiuna Yang, Kailin Yang, Xiang Liu, Luke William Guddat, Gengfu Xiao, Leike Zhang, Haitao Yang, Zihe Rao

Posted 09 Apr 2020
bioRxiv DOI: 10.1101/2020.04.09.033233 (published DOI: 10.1038/s41594-020-0440-6)

The antineoplastic drug Carmofur was shown to inhibit 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 it is a promising lead compound to develop new antiviral treatment for COVID-19. ### Competing Interest Statement The authors have declared no competing interest.

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