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About:
The dimer interface of the SARS coronavirus nucleocapsid protein adapts a porcine respiratory and reproductive syndrome virus-like structure
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An Entity of Type :
schema:ScholarlyArticle
, within Data Space :
covidontheweb.inria.fr
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document(s)
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
The dimer interface of the SARS coronavirus nucleocapsid protein adapts a porcine respiratory and reproductive syndrome virus-like structure
Creator
Chang, Chung-Ke
Huang, Tai-Huang
Chang, Chi-Fon
Chiang, Yen-Chieh
Hsieh, Chiu-Min
Sue, Shih-Che
Tsai, Cheng-Kun
Wu, Wen-Jin
De La Rosa, Miguel
Hsiao, Hsin-Hao
Lee, Shin-Jye
Yu, Tsan-Hung
Source
Elsevier; Medline; PMC
abstract
We have employed NMR to investigate the structure of SARS coronavirus nucleocapsid protein dimer. We found that the secondary structure of the dimerization domain consists of five α helices and a β-hairpin. The dimer interface consists of a continuous four-stranded β-sheet superposed by two long α helices, reminiscent of that found in the nucleocapsid protein of porcine respiratory and reproductive syndrome virus. Extensive hydrogen bond formation between the two hairpins and hydrophobic interactions between the β-sheet and the α helices render the interface highly stable. Sequence alignment suggests that other coronavirus may share the same structural topology.
has issue date
2005-10-24
(
xsd:dateTime
)
bibo:doi
10.1016/j.febslet.2005.09.038
bibo:pmid
16214138
has license
no-cc
sha1sum (hex)
06c068c68b80eaea851387c1d9a8f2ca00002105
schema:url
https://doi.org/10.1016/j.febslet.2005.09.038
resource representing a document's title
The dimer interface of the SARS coronavirus nucleocapsid protein adapts a porcine respiratory and reproductive syndrome virus-like structure
has PubMed Central identifier
PMC7094587
has PubMed identifier
16214138
schema:publication
FEBS Lett
resource representing a document's body
covid:06c068c68b80eaea851387c1d9a8f2ca00002105#body_text
is
schema:about
of
named entity 'PROTEIN '
named entity 'SARS CORONAVIRUS'
named entity 'SHEET'
named entity 'NUCLEOCAPSID PROTEIN'
named entity 'STABLE'
named entity 'SARS CORONAVIRUS'
named entity 'HIGHLY'
named entity 'STRUCTURE'
named entity 'SEQUENCE ALIGNMENT'
named entity 'EXTENSIVE'
covid:arg/06c068c68b80eaea851387c1d9a8f2ca00002105
named entity 'TOPOLOGY'
named entity 'SHARE'
named entity 'CORONAVIRUS'
named entity 'TO INVESTIGATE'
named entity 'HYDROGEN BOND'
named entity 'INTERACTIONS'
named entity 'STRUCTURE'
named entity 'INTERFACE'
named entity 'RENDER'
named entity 'SECONDARY STRUCTURE'
named entity 'DIMER'
named entity 'PORCINE RESPIRATORY AND REPRODUCTIVE SYNDROME VIRUS'
named entity 'LIKE'
named entity 'NUCLEOCAPSID PROTEIN'
named entity 'PORCINE RESPIRATORY AND REPRODUCTIVE SYNDROME VIRUS'
named entity 'HELICES'
named entity 'CONTINUOUS'
named entity 'EMPLOYED'
named entity 'DOMAIN'
named entity 'HYDROPHOBIC'
named entity 'NMR'
named entity 'INTERFACE'
named entity 'DIMER'
named entity 'STRUCTURAL'
named entity 'FORMATION'
named entity 'DIMERIZATION'
named entity 'FOUND'
named entity 'PROTEIN '
named entity 'LONG'
named entity 'HAVE'
named entity 'NMR'
named entity 'SARS coronavirus'
named entity 'hydrophobic interactions'
named entity 'hydrogen bond'
named entity 'nucleocapsid protein'
named entity 'secondary structure'
named entity 'dimerization'
named entity 'porcine'
named entity 'nucleocapsid protein'
named entity 'nucleocapsid protein'
named entity 'virus'
named entity 'porcine'
named entity 'dimer'
named entity 'Protein'
named entity 'dimer'
named entity 'NaCl'
named entity 'porcine'
named entity 'monomers'
named entity 'cross-linker'
named entity 'viruses'
named entity 'hydrophobic interactions'
named entity 'Protein'
named entity 'triple-resonance'
named entity 'SARS-CoV'
named entity 'protein'
named entity 'dimer'
named entity 'nucleocapsid proteins'
named entity 'coronavirus'
named entity 'NMR'
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