PT  - JOURNAL ARTICLE
AU  - Sisi Kang
AU  - Mei Yang
AU  - Zhongsi Hong
AU  - Liping Zhang
AU  - Zhaoxia Huang
AU  - Xiaoxue Chen
AU  - Suhua He
AU  - Ziliang Zhou
AU  - Zhechong Zhou
AU  - Qiuyue Chen
AU  - Yan Yan
AU  - Changsheng Zhang
AU  - Hong Shan
AU  - Shoudeng Chen
TI  - Crystal structure of SARS-CoV-2 nucleocapsid protein RNA binding domain reveals potential unique drug targeting sites
AID  - 10.1101/2020.03.06.977876
DP  - 2020 Jan 01
TA  - bioRxiv
PG  - 2020.03.06.977876
4099  - http://biorxiv.org/content/early/2020/03/11/2020.03.06.977876.short
4100  - http://biorxiv.org/content/early/2020/03/11/2020.03.06.977876.full
AB  - The outbreak of coronavirus disease (COVID-19) in China caused by SARS-CoV-2 virus continually lead to worldwide human infections and deaths. It is currently no specific viral protein targeted therapeutics yet. 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 is yet to be clear. Herein, we have determined the 2.7 Å crystal structure of the N-terminal RNA binding domain of SARS-CoV-2 nucleocapsid protein. Although overall structure is similar with 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.