中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
Antiviral drug design based on structural insights into the N-terminal domain and C-terminal domain of the SARS-CoV-2 nucleocapsid protein

文献类型:期刊论文

作者Luan, Xiaodong2,3,4; Li, Xinming4,6,7; Li, Yufan2,3; Su, Gengchen2,3; Yin, Wanchao8; Jiang, Yi8; Xu, Ning6,7; Wang, Feng5; Cheng, Wang5; Jin, Ye3
刊名SCIENCE BULLETIN
出版日期2022-11-30
卷号67期号:22页码:2327-2335
关键词SARS-CoV-2 Nucleocapsid protein N-terminal domain Ceftriaxone sodium
ISSN号2095-9273
DOI10.1016/j.scib.2022.10.021
通讯作者Xu, H. Eric(eric.xu@simm.ac.cn) ; Xue, Yi(yixue@mail.tsinghua.edu.cn) ; Zhang, Shuyang(shuyangzhang103@nrdrs.org)
英文摘要Nucleocapsid (N) protein plays crucial roles in the life cycle of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), including the formation of ribonucleoprotein (RNP) complex with the viral RNA. Here we reported the crystal structures of the N-terminal domain (NTD) and C-terminal domain (CTD) of the N protein and an NTD-RNA complex. Our structures reveal a unique tetramer organization of NTD and identify a distinct RNA binding mode in the NTD-RNA complex, which could contribute to the formation of the RNP complex. We also screened small molecule inhibitors of N-NTD and N-CTD and discovered that ceftriaxone sodium, an antibiotic, can block the binding of RNA to NTD and inhibit the formation of the RNP complex. These results together could facilitate the further research of antiviral drug design targeting N protein. (c) 2022 Science China Press. Published by Elsevier B.V. and Science China Press.
WOS关键词RESPIRATORY SYNDROME-CORONAVIRUS ; DIMERIZATION DOMAIN
资助项目Beijing Natural Science Foundation[M21016] ; Chinese Academy of Medical Sciences Innovation Fund for Medical Sciences[2021-I2M-1-003] ; Chinese Academy of Medical Sciences Innovation Fund for Medical Sciences[2021-CAMS-JZ004] ; Tsinghua-Peking Center for Life Sciences[045-61020100122] ; Beijing Advanced Innovation Center for Structural Biology
WOS研究方向Science & Technology - Other Topics
语种英语
WOS记录号WOS:000910089600013
出版者ELSEVIER
源URL[http://119.78.100.183/handle/2S10ELR8/303814]  
专题中国科学院上海药物研究所
通讯作者Xu, H. Eric; Xue, Yi; Zhang, Shuyang
作者单位1.Univ Chinese Acad Sci, Beijing 100049, Peoples R China
2.Tsinghua Univ, Sch Med, Beijing 100084, Peoples R China
3.Peking Union Med Coll & Chinese Acad Med Sci, Peking Union Med Coll Hosp, Dept Cardiol, Beijing 100730, Peoples R China
4.Tsinghua Univ, Tsinghua Peking Ctr Life Sci, Beijing 100084, Peoples R China
5.WuxiBiortus Biosci Co Ltd, Jiangyin 214437, Peoples R China
6.Tsinghua Univ, Sch Life Sci, Beijing 100084, Peoples R China
7.Beijing Adv Innovat Ctr Struct Biol, Beijing 100084, Peoples R China
8.Chinese Acad Sci, Shanghai Inst Mat Med, CAS Key Lab Receptor Res, Shanghai 201203, Peoples R China
9.Chinese Acad Sci, Wuhan Inst Virol, State Key Lab Virol, Ctr Biosafety Mega Sci, Wuhan 430071, Peoples R China
推荐引用方式
GB/T 7714
Luan, Xiaodong,Li, Xinming,Li, Yufan,et al. Antiviral drug design based on structural insights into the N-terminal domain and C-terminal domain of the SARS-CoV-2 nucleocapsid protein[J]. SCIENCE BULLETIN,2022,67(22):2327-2335.
APA Luan, Xiaodong.,Li, Xinming.,Li, Yufan.,Su, Gengchen.,Yin, Wanchao.,...&Zhang, Shuyang.(2022).Antiviral drug design based on structural insights into the N-terminal domain and C-terminal domain of the SARS-CoV-2 nucleocapsid protein.SCIENCE BULLETIN,67(22),2327-2335.
MLA Luan, Xiaodong,et al."Antiviral drug design based on structural insights into the N-terminal domain and C-terminal domain of the SARS-CoV-2 nucleocapsid protein".SCIENCE BULLETIN 67.22(2022):2327-2335.

入库方式: OAI收割

来源:上海药物研究所

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