Crystal structure of SARS-CoV-2 nucleocapsid protein RNA binding domain reveals potential unique dru

• 作 者: Sisi Kang Mei Yang Zhongsi Hong Liping Zhang Zhaoxia Huang Xiaoxue Chen Suhua He Ziliang Zhou Zhechong Zhou Qiuyue Chen Yan Yan Changsheng Zhang Hong Shan Shoudeng Chen
• 机 构: Molecular Imaging Center, Guangdong Provincial Key Laboratory of Biomedical Imaging, the Fifth Affil
• 出 处: 药学学报（英文版）
• 发表日期: 2020年7期
• 关键词: COVID-19 Coronavirus SARS-CoV-2 Nucleocapsid protein RNA binding domain Crystal

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 theβ-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.