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

  1. Zhenming Jin
  2. Yao Zhao
  3. Yuan Sun
  4. Bing Zhang
  5. Haofeng Wang
  6. Yan Wu
  7. Yan Zhu
  8. Chen Zhu
  9. Tianyu Hu
  10. Xiaoyu Du
  11. Yinkai Duan
  12. Jing Yu
  13. Xiaobao Yang
  14. Xiuna Yang
  15. Kailin Yang
  16. Xiang Liu
  17. Luke W. Guddat
  18. Gengfu Xiao
  19. Leike Zhang
  20. Haitao Yang
  21. Zihe Rao
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Abstract

The antineoplastic drug Carmofur was shown to inhibit SARS-CoV-2 main protease (Mpro). Here the X-ray crystal structure of Mproin 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.

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