About: Structure of the SARS Coronavirus Nucleocapsid Protein RNA-binding Dimerization Domain Suggests a Mechanism for Helical Packaging of Viral RNA

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About: Structure of the SARS Coronavirus Nucleocapsid Protein RNA-binding Dimerization Domain Suggests a Mechanism for Helical Packaging of Viral RNA Goto Sponge NotDistinct Permalink

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	Structure of the SARS Coronavirus Nucleocapsid Protein RNA-binding Dimerization Domain Suggests a Mechanism for Helical Packaging of Viral RNA
Creator	Chang, Chung-Ke Huang, Tai-Huang Hsiao, Chwan-Deng Sue, Shih-Che Bai, Hsin-I Chang, Yi-Wei Chen, Chun-Yuan Riang, Lilianty
source	Elsevier; Medline; PMC
abstract	Abstract Coronavirus nucleocapsid proteins are basic proteins that encapsulate viral genomic RNA to form part of the virus structure. The nucleocapsid protein of SARS-CoV is highly antigenic and associated with several host-cell interactions. Our previous studies using nuclear magnetic resonance revealed the domain organization of the SARS-CoV nucleocapsid protein. RNA has been shown to bind to the N-terminal domain (NTD), although recently the C-terminal half of the protein has also been implicated in RNA binding. Here, we report that the C-terminal domain (CTD), spanning residues 248–365 (NP248-365), had stronger nucleic acid-binding activity than the NTD. To determine the molecular basis of this activity, we have also solved the crystal structure of the NP248-365 region. Residues 248–280 form a positively charged groove similar to that found in the infectious bronchitis virus (IBV) nucleocapsid protein. Furthermore, the positively charged surface area is larger in the SARS-CoV construct than in the IBV. Interactions between residues 248–280 and the rest of the molecule also stabilize the formation of an octamer in the asymmetric unit. Packing of the octamers in the crystal forms two parallel, basic helical grooves, which may be oligonucleotide attachment sites, and suggests a mechanism for helical RNA packaging in the virus.
has issue date	2007-05-11(xsd:dateTime)
bibo:doi	10.1016/j.jmb.2007.02.069
bibo:pmid	17379242
has license	els-covid
sha1sum (hex)	1ea6be4eecf0093e81b682161122e234bef6b6c0
schema:url	https://doi.org/10.1016/j.jmb.2007.02.069
resource representing a document's title	Structure of the SARS Coronavirus Nucleocapsid Protein RNA-binding Dimerization Domain Suggests a Mechanism for Helical Packaging of Viral RNA
has PubMed Central identifier	PMC7094638
has PubMed identifier	17379242
schema:publication	Journal of Molecular Biology
resource representing a document's body	covid:1ea6be4eecf0093e81b682161122e234bef6b6c0#body_text
is schema:about of	named entity 'PACKAGING' named entity 'SARS CORONAVIRUS' named entity 'MECHANISM' named entity 'PROTEIN ' named entity 'NUCLEOCAPSID PROTEINS' named entity 'NUCLEAR MAGNETIC RESONANCE' named entity 'ENCAPSULATE' named entity 'SARS-COV' named entity 'PROTEIN ' named entity 'USING' named entity 'ASSOCIATED WITH' named entity 'GENOMIC' named entity 'REVEALED' named entity 'ORGANIZATION' named entity 'OUR' named entity 'DOMAIN' named entity 'RNA' named entity 'RNA' named entity 'PROTEINS' named entity 'BASIC' named entity 'TO FORM' named entity 'PART OF' named entity 'VIRAL RNA' named entity 'BINDING' named entity 'NUCLEOCAPSID PROTEIN' named entity 'DIMERIZATION' named entity 'STRUCTURE' named entity 'INTERACTIONS' named entity 'STUDIES' named entity 'CORONAVIRUS' named entity 'NUCLEOCAPSID PROTEIN' named entity 'STRUCTURE' named entity 'HELICAL' named entity 'HOST' named entity 'CELL' named entity 'PREVIOUS' named entity 'VIRUS' named entity 'HIGHLY' named entity 'VIRAL' named entity 'DOMAIN' named entity 'Coronavirus' named entity 'RNA-binding' named entity 'RNA' named entity 'SARS' named entity 'diffracted' named entity 'crystal form' named entity 'atom' named entity 'protein' named entity 'N-terminal' named entity 'MgSO' named entity 'nucleocapsid' named entity 'oligomers' named entity 'oligonucleotides' named entity 'binding site' named entity 'Arteriviridae' named entity 'coronaviruses' named entity 'nucleocapsid' named entity 'assay' named entity 'ClustalW' named entity 'host-cell' named entity 'coronavirus' named entity 'ssDNA' named entity 'NMR spectra' named entity 'B12' named entity 'secondary structure' named entity 'nucleocapsid protein' named entity 'cellular processes' named entity 'RNA' named entity 'protein' named entity 'ssDNA' named entity 'binding site' named entity 'viruses' named entity 'SARS-CoV' named entity 'stem-loop'

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