SrasV1, Main, Exploration, bibRecord, 002048

SARS-CoV heptad repeat 2 is a trimer of parallel helices.

Identifieur interne : 002048 ( Main/Exploration ); précédent : 002047; suivant : 002049

SARS-CoV heptad repeat 2 is a trimer of parallel helices.

Auteurs : Jessica Celigoy [États-Unis] ; Benjamin Ramirez ; Michael Caffrey

Source :

Protein science : a publication of the Protein Society [ 1469-896X ] ; 2011.

RBID : pubmed:21922588

Descripteurs français

KwdFr :
- Marqueurs de spin, Modèles moléculaires, Multimérisation de protéines, Protéines de l'enveloppe virale (), Résonance magnétique nucléaire biomoléculaire, Structure secondaire des protéines, Syndrome respiratoire aigu sévère (virologie), Virus du SRAS ().
MESH :
- virologie : Syndrome respiratoire aigu sévère.
- Marqueurs de spin, Modèles moléculaires, Multimérisation de protéines, Protéines de l'enveloppe virale, Résonance magnétique nucléaire biomoléculaire, Structure secondaire des protéines, Virus du SRAS.

English descriptors

KwdEn :
- Models, Molecular, Nuclear Magnetic Resonance, Biomolecular, Protein Multimerization, Protein Structure, Secondary, SARS Virus (chemistry), Severe Acute Respiratory Syndrome (virology), Spin Labels, Viral Envelope Proteins (chemistry).
MESH :
- chemical , chemistry : Viral Envelope Proteins.
- chemical : Spin Labels.
- chemistry : SARS Virus.
- virology : Severe Acute Respiratory Syndrome.
- Models, Molecular, Nuclear Magnetic Resonance, Biomolecular, Protein Multimerization, Protein Structure, Secondary.

Abstract

In severe acute respiratory syndrome coronavirus, the envelope heptad repeat 2 (HR2) plays a critical role in viral entry. Moreover, HR2 is both the target for novel antiviral therapies and, as an isolated peptide, presents a potential antiviral therapeutic. The structure of HR2, as determined by NMR spectroscopy in the presence of the co-solvent trifluoroethanol (TFE), is a trimer of parallel helices, whereas the structure of HR2, as determined by X-ray crystallography, is a tetramer of anti-parallel helices. In this work, we added a nitroxide spin label to the N-terminal region of HR2 and used paramagnetic relaxation enhancement to assess the orientation of the HR2 helices under different solution conditions. We find that the relaxation effects are consistent with an orientation corresponding to a trimer of parallel helices in both the presence and absence of TFE. This work suggests that the different orientation and oligomerization states observed by NMR and X-ray are due to the 11 additional residues present at the N-terminus of the NMR construct.

DOI: 10.1002/pro.736
PubMed: 21922588

Affiliations:

Le document en format XML

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<front><div type="abstract" xml:lang="en">In severe acute respiratory syndrome coronavirus, the envelope heptad repeat 2 (HR2) plays a critical role in viral entry. Moreover, HR2 is both the target for novel antiviral therapies and, as an isolated peptide, presents a potential antiviral therapeutic. The structure of HR2, as determined by NMR spectroscopy in the presence of the co-solvent trifluoroethanol (TFE), is a trimer of parallel helices, whereas the structure of HR2, as determined by X-ray crystallography, is a tetramer of anti-parallel helices. In this work, we added a nitroxide spin label to the N-terminal region of HR2 and used paramagnetic relaxation enhancement to assess the orientation of the HR2 helices under different solution conditions. We find that the relaxation effects are consistent with an orientation corresponding to a trimer of parallel helices in both the presence and absence of TFE. This work suggests that the different orientation and oligomerization states observed by NMR and X-ray are due to the 11 additional residues present at the N-terminus of the NMR construct.</div>
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<country name="États-Unis"><region name="Illinois"><name sortKey="Celigoy, Jessica" sort="Celigoy, Jessica" uniqKey="Celigoy J" first="Jessica" last="Celigoy">Jessica Celigoy</name>
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Serveur d'exploration SRAS

SARS-CoV heptad repeat 2 is a trimer of parallel helices.

SARS-CoV heptad repeat 2 is a trimer of parallel helices.

Source :

Descripteurs français

English descriptors

Abstract

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

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki

	Serveur d'exploration SRAS
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