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Crystal structure of SARS-CoV-2 nucleocapsid protein RNA binding domain reveals potential unique drug targeting sites

Acta pharmaceutica Sinica. B, 2020-07, Vol.10 (7), p.1228-1238 [Peer Reviewed Journal]

2020 Chinese Pharmaceutical Association and Institute of Materia Medica, Chinese Academy of Medical Sciences ;2020 Chinese Pharmaceutical Association and Institute of Materia Medica, Chinese Academy of Medical Sciences. Production and hosting by Elsevier B.V. ;2020 Chinese Pharmaceutical Association and Institute of Materia Medica, Chinese Academy of Medical Sciences. Production and hosting by Elsevier B.V. 2020 Chinese Pharmaceutical Association and Institute of Materia Medica, Chinese Academy of Medical Sciences ;ISSN: 2211-3835 ;EISSN: 2211-3843 ;DOI: 10.1016/j.apsb.2020.04.009 ;PMID: 32363136

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  • Title:
    Crystal structure of SARS-CoV-2 nucleocapsid protein RNA binding domain reveals potential unique drug targeting sites
  • Author: Kang, Sisi ; Yang, Mei ; Hong, Zhongsi ; Zhang, Liping ; Huang, Zhaoxia ; Chen, Xiaoxue ; He, Suhua ; Zhou, Ziliang ; Zhou, Zhechong ; Chen, Qiuyue ; Yan, Yan ; Zhang, Changsheng ; Shan, Hong ; Chen, Shoudeng
  • Subjects: Antiviral targeting site ; Coronavirus ; COVID-19 ; Crystal structure ; Nucleocapsid protein ; Original article ; RNA binding domain ; SARS-CoV-2
  • Is Part Of: Acta pharmaceutica Sinica. B, 2020-07, Vol.10 (7), p.1228-1238
  • Description: The outbreak of coronavirus disease (COVID-19) caused by SARS-CoV-2 virus continually lead to worldwide human infections and deaths. Currently, there is no specific viral protein-targeted therapeutics. Viral nucleocapsid protein is a potential antiviral drug target, serving multiple critical functions during the viral life cycle. However, the structural information of SARS-CoV-2 nucleocapsid protein remains unclear. Herein, we have determined the 2.7 Å crystal structure of the N-terminal RNA binding domain of SARS-CoV-2 nucleocapsid protein. Although the overall structure is similar as other reported coronavirus nucleocapsid protein N-terminal domain, the surface electrostatic potential characteristics between them are distinct. Further comparison with mild virus type HCoV-OC43 equivalent domain demonstrates a unique potential RNA binding pocket alongside the β-sheet core. Complemented by in vitro binding studies, our data provide several atomic resolution features of SARS-CoV-2 nucleocapsid protein N-terminal domain, guiding the design of novel antiviral agents specific targeting to SARS-CoV-2. The crystal structure of the N-terminal RNA-binding domain of SARS-CoV-2 nucleocapsid protein was determined by X-ray. Compared with other previously reported coronavirus nucleocapsid protein N-terminal domains, the authors have identified a unique potential RNA-binding pocket that can guide the design of novel antiviral drugs targeting SARS-CoV-2. [Display omitted]
  • Publisher: Netherlands: Elsevier B.V
  • Language: English
  • Identifier: ISSN: 2211-3835
    EISSN: 2211-3843
    DOI: 10.1016/j.apsb.2020.04.009
    PMID: 32363136
  • Source: Open Access: DOAJ Directory of Open Access Journals
    Open Access: PubMed Central
    Geneva Foundation Free Medical Journals at publisher websites
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