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

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.


The opinions expressed here are the views of the writer and do not necessarily reflect the views and opinions of News Medical.
Post a new comment
You might also like...
Impact of prior SARS-CoV-2 infection and mRNA vaccination on contagiousness and infection risk