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About:
Crystal structure of SARS-CoV-2 nucleocapsid protein RNA binding domain reveals potential unique drug targeting sites
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wasabi.inria.fr
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Type:
Academic Article
research paper
schema:ScholarlyArticle
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type
Academic Article
research paper
schema:ScholarlyArticle
isDefinedBy
Covid-on-the-Web dataset
has title
Crystal structure of SARS-CoV-2 nucleocapsid protein RNA binding domain reveals potential unique drug targeting sites
Creator
Hong, Zhongsi
Shan, Hong
Yan, Yan
Zhang, Liping
Zhang, Changsheng
Chen, Qiuyue
Chen, Shoudeng
Chen, Xiaoxue
He, Suhua
Huang, Zhaoxia
Kang, Sisi
Yang, Mei
Zhou, Zhechong
Zhou, Ziliang
Source
BioRxiv; MedRxiv
abstract
The outbreak of coronavirus disease (COVID-19) in China caused by SARS-CoV-2 virus continually lead to worldwide human infections and deaths. It is currently no specific viral protein targeted therapeutics yet. 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 is yet to be clear. Herein, we have determined the 2.7 Å crystal structure of the N-terminal RNA binding domain of SARS-CoV-2 nucleocapsid protein. Although overall structure is similar with 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.
has issue date
2020-03-07
(
xsd:dateTime
)
bibo:doi
10.1101/2020.03.06.977876
has license
biorxiv
sha1sum (hex)
854a29cd858f64982c799eb27c0a45cb762adfa8
schema:url
https://doi.org/10.1101/2020.03.06.977876
resource representing a document's title
Crystal structure of SARS-CoV-2 nucleocapsid protein RNA binding domain reveals potential unique drug targeting sites
schema:publication
bioRxiv
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covid:854a29cd858f64982c799eb27c0a45cb762adfa8#body_text
is
schema:about
of
named entity 'outbreak'
named entity 'OUTBREAK'
named entity 'nucleocapsid'
named entity 'reveals'
named entity 'outbreak of coronavirus'
named entity 'drug targeting'
named entity 'SARS-CoV-2'
named entity 'nucleocapsid protein'
named entity 'RNA binding'
named entity 'peer-reviewed'
named entity 'apoptosis'
named entity 'bioRxiv'
named entity 'preprint'
named entity 'pathogen'
named entity 'preprint'
named entity 'preprint'
named entity 'Electrostatic'
named entity 'genome'
named entity 'GE Healthcare'
named entity 'preprint'
named entity 'plasmid'
named entity 'helical'
named entity 'nucleocapsid'
named entity 'ribonucleoside'
named entity 'SARS-CoV'
named entity 'nucleocapsid'
named entity 'bioRxiv'
named entity 'Rigaku'
named entity 'protein'
named entity 'host cell'
named entity 'antibody-dependent enhancement'
named entity 'nitrogenous base'
named entity 'SARS-CoV'
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named entity 'HCoV-OC43'
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named entity 'peer-reviewed'
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named entity 'phosphate group'
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named entity 'Guangdong'
named entity 'transcription'
named entity 'Protein Data Bank'
named entity 'SARS-CoV-2'
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named entity 'MERS-CoV'
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named entity 'proteases'
named entity 'OC43'
named entity 'nucleocapsid'
named entity 'column chromatography'
named entity 'SARS-CoV-2'
named entity 'SARS-CoV-2'
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