Crystal structure of SARS-CoV-2 nucleocapsid protein RNA binding domain reveals potential unique drug targeting sites.
Antiviral targeting site
COVID-19
Coronavirus
Crystal structure
Nucleocapsid protein
RNA binding domain
SARS-CoV-2
Journal
Acta pharmaceutica Sinica. B
ISSN: 2211-3835
Titre abrégé: Acta Pharm Sin B
Pays: Netherlands
ID NLM: 101600560
Informations de publication
Date de publication:
Jul 2020
Jul 2020
Historique:
received:
04
03
2020
revised:
19
03
2020
accepted:
31
03
2020
pubmed:
5
5
2020
medline:
5
5
2020
entrez:
5
5
2020
Statut:
ppublish
Résumé
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
Identifiants
pubmed: 32363136
doi: 10.1016/j.apsb.2020.04.009
pii: S2211-3835(20)30550-5
pmc: PMC7194921
doi:
Types de publication
Journal Article
Langues
eng
Pagination
1228-1238Informations de copyright
© 2020 Chinese Pharmaceutical Association and Institute of Materia Medica, Chinese Academy of Medical Sciences. Production and hosting by Elsevier B.V.
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