About: Transient Oligomerization of the SARS-CoV N Protein – Implication for Virus Ribonucleoprotein Packaging

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About: Transient Oligomerization of the SARS-CoV N Protein – Implication for Virus Ribonucleoprotein Packaging Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Transient Oligomerization of the SARS-CoV N Protein – Implication for Virus Ribonucleoprotein Packaging
Creator	Chen, C-K Chiang, C-Mm Hsu, M-H Huang, Y-L
Source	Medline; PMC
abstract	The nucleocapsid (N) phosphoprotein of the severe acute respiratory syndrome coronavirus (SARS-CoV) packages the viral genome into a helical ribonucleocapsid and plays a fundamental role during viral self-assembly. The N protein consists of two structural domains interspersed between intrinsically disordered regions and dimerizes through the C-terminal structural domain (CTD). A key activity of the protein is the ability to oligomerize during capsid formation by utilizing the dimer as a building block, but the structural and mechanistic bases of this activity are not well understood. By disulfide trapping technique we measured the amount of transient oligomers of N protein mutants with strategically located cysteine residues and showed that CTD acts as a primary transient oligomerization domain in solution. The data is consistent with the helical oligomer packing model of N protein observed in crystal. A systematic study of the oligomerization behavior revealed that altering the intermolecular electrostatic repulsion through changes in solution salt concentration or phosphorylation-mimicking mutations affects oligomerization propensity. We propose a biophysical mechanism where electrostatic repulsion acts as a switch to regulate N protein oligomerization.
has issue date	2013-05-23(xsd:dateTime)
bibo:doi	10.1371/journal.pone.0065045
bibo:pmid	23717688
has license	cc-by
sha1sum (hex)	054e3e247ad11de2be71be7215e30a44222271ab
schema:url	https://doi.org/10.1371/journal.pone.0065045
resource representing a document's title	Transient Oligomerization of the SARS-CoV N Protein – Implication for Virus Ribonucleoprotein Packaging
has PubMed Central identifier	PMC3662775
has PubMed identifier	23717688
schema:publication	PLoS One
resource representing a document's body	covid:054e3e247ad11de2be71be7215e30a44222271ab#body_text
is schema:about of	named entity 'VIRUS' named entity 'TRANSIENT' named entity 'PACKING' named entity 'MUTANTS' named entity 'CONSISTENT WITH' named entity 'OLIGOMERIZATION' named entity 'SARS-COV' named entity 'CTD' named entity 'DATA' named entity 'OLIGOMER' named entity 'TRANSIENT' named entity 'PROTEIN ' named entity 'MEASURED' named entity 'DIMER' named entity 'SWITCH' named entity 'MECHANISM' named entity 'BEHAVIOR' named entity 'CONCENTRATION' named entity 'TECHNIQUE' named entity 'N PROTEIN' named entity 'ACTS' named entity 'SOLUTION' named entity 'ELECTROSTATIC' named entity 'PACKAGES' named entity 'NOT WELL' named entity 'N PROTEIN' named entity 'RIBONUCLEOPROTEIN' named entity 'ROLE' named entity 'CRYSTAL' named entity 'PRIMARY' named entity 'VIRAL GENOME' named entity 'STRUCTURAL' named entity 'MODEL OF' named entity 'TRAPPING' named entity 'STRUCTURAL DOMAIN' named entity 'OLIGOMERS' named entity 'SALT' named entity 'BIOPHYSICAL' named entity 'HELICAL' named entity 'VIRAL' named entity 'DISULFIDE' named entity 'REPULSION' named entity 'TO REGULATE' named entity 'WHERE' named entity 'SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS' named entity 'PHOSPHOPROTEIN' named entity 'DISORDERED' named entity 'MUTATIONS' named entity 'UNDERSTOOD' named entity 'CAPSID FORMATION' named entity 'PHOSPHORYLATION' named entity 'C-TERMINAL' named entity 'DOMAIN' named entity 'STUDY' named entity 'KEY' named entity 'PROTEIN OLIGOMERIZATION' named entity 'REGIONS' named entity 'REVEALED' named entity 'CHANGES' named entity 'ACTIVITY' named entity 'OLIGOMERIZATION' named entity 'BUT' named entity 'CYSTEINE' named entity 'OBSERVED' named entity 'SELF-ASSEMBLY' named entity 'PACKAGING' named entity 'PROTEIN ' named entity 'NUCLEOCAPSID' named entity 'BASES' named entity 'PLAYS' named entity 'ALTERING' covid:arg/054e3e247ad11de2be71be7215e30a44222271ab named entity 'intrinsically disordered regions' named entity 'dimerizes' named entity 'oligomerization' named entity 'oligomerization' named entity 'oligomer' named entity 'nucleocapsid'

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