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Crystal structure of SARS-CoV-2 nucleocapsid protein RNA binding domain could guide design of antiviral agents - News-Medical.net

The outbreak of coronavirus disease (COVID-19) caused by SARS-CoV-2 virus continues to cause human infection and mortality worldwide. Currently, there are no specific viral protein-targeted therapeutics available.

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.

In this article, the authors 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, the authors data provides several atomic resolution features of SARS-CoV-2 nucleocapsid protein N-terminal domain, which could guide the design of novel antiviral agents specifically targeting to SARS-CoV-2.

Journal reference:

Kang, S., et al. (2020) Crystal structure of SARS-CoV-2 nucleocapsid protein RNA binding domain reveals potential unique drug targeting sites. Acta Pharmaceutica Sinica B. doi.org/10.1016/j.apsb.2020.04.009.

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2020-10-20 14:04:00Z
CBMingFodHRwczovL3d3dy5uZXdzLW1lZGljYWwubmV0L25ld3MvMjAyMDEwMjAvQ3J5c3RhbC1zdHJ1Y3R1cmUtb2YtU0FSUy1Db1YtMi1udWNsZW9jYXBzaWQtcHJvdGVpbi1STkEtYmluZGluZy1kb21haW4tY291bGQtZ3VpZGUtZGVzaWduLW9mLWFudGl2aXJhbC1hZ2VudHMuYXNweNIBogFodHRwczovL3d3dy5uZXdzLW1lZGljYWwubmV0L2FtcC9uZXdzLzIwMjAxMDIwL0NyeXN0YWwtc3RydWN0dXJlLW9mLVNBUlMtQ29WLTItbnVjbGVvY2Fwc2lkLXByb3RlaW4tUk5BLWJpbmRpbmctZG9tYWluLWNvdWxkLWd1aWRlLWRlc2lnbi1vZi1hbnRpdmlyYWwtYWdlbnRzLmFzcHg

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