Article: Crystal structure of SARS-CoV-2 nucleocapsid protein RNA binding domain reveals potential unique drug targeting sites.
Acta pharmaceutica Sinica. B
2020 Volume 10, Issue 7, Page(s) 1228–1238
Abstract: ... domain of SARS-CoV-2 nucleocapsid protein. Although the overall structure is similar as other reported ... remains unclear. Herein, we have determined the 2.7 Å crystal structure of the N-terminal RNA binding ... during the viral life cycle. However, the structural information of SARS-CoV-2 nucleocapsid protein ...
| Abstract | 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 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 |
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| Keywords | covid19 |
| Language | English |
| Publishing date | 2020-04-20 |
| Publishing country | Netherlands |
| Document type | Journal Article |
| ISSN | 2211-3835 |
| ISSN | 2211-3835 |
| DOI | 10.1016/j.apsb.2020.04.009 |
| Database | MEDical Literature Analysis and Retrieval System OnLINE |
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