Structural basis for the inhibition of SARS-CoV-2 main protease by antineoplastic drug carmofur
Structural basis for the inhibition of SARS-CoV-2 main protease by antineoplastic drug carmofur
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Jin, Zhenming , Zhao, Yao , Sun, Yuan , Zhang, Bing , Wang, Haofeng , Wu, Yan , Zhu, Yan , Zhu, Chen , Hu, Tianyu , Du, Xiaoyu , Duan, Yinkai , Yu, Jing , Yang, Xiaobao , Yang, Xiuna , Yang, Kailin , Liu, Xiang , Guddat, Luke W. , Xiao, Gengfu , Zhang, Leike , Yang, Haitao and Rao, Zihe
Publisher
New York: Nature Publishing Group US
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English
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Publisher
New York: Nature Publishing Group US
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Contents
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 v...
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Full title
Structural basis for the inhibition of SARS-CoV-2 main protease by antineoplastic drug carmofur
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TN_cdi_proquest_journals_2412192729
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_2412192729
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ISSN
1545-9993
E-ISSN
1545-9985
DOI
10.1038/s41594-020-0440-6
