Structural basis for the inhibition of SARS-CoV-2 main protease by antineoplastic drug carmofur.,Nature Structural & Molecular Biology

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Structural basis for the inhibition of SARS-CoV-2 main protease by antineoplastic drug carmofur.
Nature Structural & Molecular Biology ( IF 16.8 ) Pub Date : 2020-05-07 , DOI: 10.1038/s41594-020-0440-6
Zhenming Jin _{1,

2} , Yao Zhao ₁ , Yuan Sun ₃ , Bing Zhang ₁ , Haofeng Wang _{1,

4} , Yan Wu ₃ , Yan Zhu ₁ , Chen Zhu ₁ , Tianyu Hu ₁ , Xiaoyu Du _{1,

2} , Yinkai Duan ₁ , Jing Yu ₁ , Xiaobao Yang ₁ , Xiuna Yang ₁ , Kailin Yang ₅ , Xiang Liu ₆ , Luke W Guddat ₇ , Gengfu Xiao ₃ , Leike Zhang ₃ , Haitao Yang ₁ , Zihe Rao _{1,

2,

6}

Affiliation

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.

中文翻译：

抗肿瘤药物卡莫氟抑制 SARS-CoV-2 主蛋白酶的结构基础。

抗肿瘤药物卡莫氟显示出可抑制 SARS-CoV-2 主要蛋白酶 (Mpro)。在这里，与卡莫氟复合的 Mpro 的 X 射线晶体结构表明，卡莫氟的羰基反应基团与催化性 Cys145 共价结合，而其脂肪酸尾部占据疏水性 S2 亚位点。Carmofur 抑制细胞中的病毒复制 (EC50 = 24.30 μM)，是开发 COVID-19 新抗病毒治疗的有前途的先导化合物。

更新日期：2020-05-07

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