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10.1016/j.apsb.2020.04.009

http://scihub22266oqcxt.onion/10.1016/j.apsb.2020.04.009
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32363136!7194921!32363136
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suck abstract from ncbi

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  • Crystal structure of SARS-CoV-2 nucleocapsid protein RNA binding domain reveals potential unique drug targeting sites #MMPMID32363136
  • Kang S; Yang M; Hong Z; Zhang L; Huang Z; Chen X; He S; Zhou Z; Zhou Z; Chen Q; Yan Y; Zhang C; Shan H; Chen S
  • Acta Pharm Sin B 2020[Jul]; 10 (7): 1228-1238 PMID32363136show ga
  • 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 A 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 beta-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.
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  • suck abstract from ncbi

    1228 7.10 2020