tetano
Editor, Senior Moderator
Acta Pharm Sin B. 2020 Apr 20. doi: 10.1016/j.apsb.2020.04.009. [Epub ahead of print]
Crystal structure of SARS-CoV-2 nucleocapsid protein RNA binding domain reveals potential unique drug targeting sites.
Kang S[SUP]1[/SUP], Yang M[SUP]1[/SUP], Hong Z[SUP]2[/SUP], Zhang L[SUP]3[/SUP], Huang Z[SUP]1[/SUP], Chen X[SUP]1[/SUP], He S[SUP]1[/SUP], Zhou Z[SUP]1[/SUP], Zhou Z[SUP]1[/SUP], Chen Q[SUP]1[/SUP], Yan Y[SUP]1[/SUP], Zhang C[SUP]3[/SUP], Shan H[SUP]1,[/SUP][SUP]4,[/SUP][SUP]5[/SUP], Chen S[SUP]1,[/SUP][SUP]4,[/SUP][SUP]6[/SUP].
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Abstract
The outbreak of coronavirus disease (COVID-19) caused by SARS-CoV-2 virus continually led 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 ? 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, 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.
? 2020 Chinese Pharmaceutical Association and Institute of Materia Medica, Chinese Academy of Medical Sciences. Production and hosting by Elsevier B.V.
KEYWORDS:
Antiviral targeting site; COVID-19; Coronavirus; Crystal structure; Nucleocapsid protein; RNA binding domain; SARS-CoV-2
PMID:32363136PMCID:PMC7194921DOI:10.1016/j.apsb.2020.04.009
Free full text
Crystal structure of SARS-CoV-2 nucleocapsid protein RNA binding domain reveals potential unique drug targeting sites.
Kang S[SUP]1[/SUP], Yang M[SUP]1[/SUP], Hong Z[SUP]2[/SUP], Zhang L[SUP]3[/SUP], Huang Z[SUP]1[/SUP], Chen X[SUP]1[/SUP], He S[SUP]1[/SUP], Zhou Z[SUP]1[/SUP], Zhou Z[SUP]1[/SUP], Chen Q[SUP]1[/SUP], Yan Y[SUP]1[/SUP], Zhang C[SUP]3[/SUP], Shan H[SUP]1,[/SUP][SUP]4,[/SUP][SUP]5[/SUP], Chen S[SUP]1,[/SUP][SUP]4,[/SUP][SUP]6[/SUP].
Author information
Abstract
The outbreak of coronavirus disease (COVID-19) caused by SARS-CoV-2 virus continually led 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 ? 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, 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.
? 2020 Chinese Pharmaceutical Association and Institute of Materia Medica, Chinese Academy of Medical Sciences. Production and hosting by Elsevier B.V.
KEYWORDS:
Antiviral targeting site; COVID-19; Coronavirus; Crystal structure; Nucleocapsid protein; RNA binding domain; SARS-CoV-2
PMID:32363136PMCID:PMC7194921DOI:10.1016/j.apsb.2020.04.009
Free full text