SrasV1, Ncbi, Merge, bibRecord, 002605

Structure of alphacoronavirus transmissible gastroenteritis virus nsp1 has implications for coronavirus nsp1 function and evolution.

Identifieur interne : 002605 ( Ncbi/Merge ); précédent : 002604; suivant : 002606

Structure of alphacoronavirus transmissible gastroenteritis virus nsp1 has implications for coronavirus nsp1 function and evolution.

Auteurs : Anna M. Jansson [Suède]

Source :

Journal of virology [ 1098-5514 ] ; 2013.

RBID : pubmed:23269811

Descripteurs français

KwdFr :
- Alignement de séquences, Cristallographie aux rayons X, Données de séquences moléculaires, Expression des gènes, Modèles moléculaires, Pliage des protéines, Protéines virales non structurales (), Protéines virales non structurales (génétique), Protéines virales non structurales (métabolisme), RNA replicase (), RNA replicase (génétique), RNA replicase (métabolisme), Structure secondaire des protéines, Structure tertiaire des protéines, Séquence d'acides aminés, Virus de la gastroentérite transmissible (), Virus de la gastroentérite transmissible (génétique).
MESH :

English descriptors

KwdEn :
- Amino Acid Sequence, Crystallography, X-Ray, Gene Expression, Models, Molecular, Molecular Sequence Data, Protein Folding, Protein Structure, Secondary, Protein Structure, Tertiary, RNA Replicase (chemistry), RNA Replicase (genetics), RNA Replicase (metabolism), Sequence Alignment, Transmissible gastroenteritis virus (chemistry), Transmissible gastroenteritis virus (classification), Transmissible gastroenteritis virus (genetics), Viral Nonstructural Proteins (chemistry), Viral Nonstructural Proteins (genetics), Viral Nonstructural Proteins (metabolism).
MESH :
- chemical , chemistry : RNA Replicase, Viral Nonstructural Proteins.
- chemical , genetics : RNA Replicase, Viral Nonstructural Proteins.
- chemical , metabolism : RNA Replicase, Viral Nonstructural Proteins.
- chemistry : Transmissible gastroenteritis virus.
- classification : Transmissible gastroenteritis virus.
- genetics : Transmissible gastroenteritis virus.
- Amino Acid Sequence, Crystallography, X-Ray, Gene Expression, Models, Molecular, Molecular Sequence Data, Protein Folding, Protein Structure, Secondary, Protein Structure, Tertiary, Sequence Alignment.

Abstract

Coronavirus nsp1 has been shown to induce suppression of host gene expression and to interfere with the host immune response. However, the mechanism is currently unknown. The only available structural information on coronavirus nsp1 is the nuclear magnetic resonance (NMR) structure of the N-terminal domain of nsp1 from severe acute respiratory syndrome coronavirus (SARS-CoV) from the betacoronavirus genus. Here we present the first nsp1 structure from an alphacoronavirus, transmissible gastroenteritis virus (TGEV) nsp1. It displays a six-stranded β-barrel fold with a long alpha helix on the rim of the barrel, a fold shared with SARS-CoV nsp1(13-128). Contrary to previous speculation, the TGEV nsp1 structure suggests that coronavirus nsp1s have a common origin, despite the lack of sequence homology. However, comparisons of surface electrostatics, shape, and amino acid conservation between the alpha- and betacoronaviruses lead us to speculate that the mechanism for nsp1-induced suppression of host gene expression might be different in these two genera.

DOI: 10.1128/JVI.03163-12
PubMed: 23269811

Links toward previous steps (curation, corpus...)

to stream PubMed, to step Corpus: 001269
to stream PubMed, to step Curation: 001269
to stream PubMed, to step Checkpoint: 001097

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pubmed:23269811

Le document en format XML

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<affiliations><list><country><li>Suède</li>
</country>
<region><li>East Middle Sweden</li>
<li>Svealand</li>
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<settlement><li>Uppsala</li>
</settlement>
<orgName><li>Université d'Uppsala</li>
</orgName>
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<tree><country name="Suède"><region name="Svealand"><name sortKey="Jansson, Anna M" sort="Jansson, Anna M" uniqKey="Jansson A" first="Anna M" last="Jansson">Anna M. Jansson</name>
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Structure of alphacoronavirus transmissible gastroenteritis virus nsp1 has implications for coronavirus nsp1 function and evolution.

Structure of alphacoronavirus transmissible gastroenteritis virus nsp1 has implications for coronavirus nsp1 function and evolution.

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