Journal article
Structural basis for the inhibition of SARS-CoV-2 main protease by antineoplastic drug carmofur
Nature structural & molecular biology, Vol.27(6), pp.529-532
06/01/2020
DOI: 10.1038/s41594-020-0440-6
PMID: 32382072
Abstract
The antineoplastic drug carmofur is shown to inhibit the SARS-CoV-2 main protease (M
). Here, the X-ray crystal structure of M
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 (EC
= 24.30 μM) and is a promising lead compound to develop new antiviral treatment for COVID-19.
Details
- Title: Subtitle
- Structural basis for the inhibition of SARS-CoV-2 main protease by antineoplastic drug carmofur
- Creators
- Zhenming Jin - Tsinghua UniversityYao Zhao - ShanghaiTech UniversityYuan Sun - Wuhan Institute of VirologyBing Zhang - ShanghaiTech UniversityHaofeng Wang - ShanghaiTech UniversityYan Wu - Wuhan Institute of VirologyYan Zhu - ShanghaiTech UniversityChen Zhu - ShanghaiTech UniversityTianyu Hu - ShanghaiTech UniversityXiaoyu Du - ShanghaiTech UniversityYinkai Duan - ShanghaiTech UniversityJing Yu - ShanghaiTech UniversityXiaobao Yang - ShanghaiTech UniversityXiuna Yang - ShanghaiTech UniversityKailin Yang - Cleveland ClinicXiang Liu - Nankai UniversityLuke W Guddat - University of QueenslandGengfu Xiao - Wuhan Institute of VirologyLeike Zhang - Chinese Academy of SciencesHaitao Yang - ShanghaiTech UniversityZihe Rao - Nankai University
- Resource Type
- Journal article
- Publication Details
- Nature structural & molecular biology, Vol.27(6), pp.529-532
- DOI
- 10.1038/s41594-020-0440-6
- PMID
- 32382072
- ISSN
- 1545-9993
- eISSN
- 1545-9985
- Language
- English
- Date published
- 06/01/2020
- Academic Unit
- Radiation Oncology
- Record Identifier
- 9984696722402771
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