An amphipathic alpha-helix at the C terminus of hepatitis C virus nonstructural protein 4B mediates membrane association.

Détails

ID Serval
serval:BIB_579AA3CFD580
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
An amphipathic alpha-helix at the C terminus of hepatitis C virus nonstructural protein 4B mediates membrane association.
Périodique
Journal of Virology
Auteur(s)
Gouttenoire J., Montserret R., Kennel A., Penin F., Moradpour D.
ISSN
1098-5514[electronic]
Statut éditorial
Publié
Date de publication
2009
Volume
83
Numéro
21
Pages
11378-11384
Langue
anglais
Résumé
Nonstructural protein 4B (NS4B) plays an essential role in the formation of the hepatitis C virus (HCV) replication complex. It is an integral membrane protein that has been only poorly characterized to date. It is believed to comprise a cytosolic N-terminal part, a central part harboring four transmembrane passages, and a cytosolic C-terminal part. Here, we describe an amphipathic alpha-helix at the C terminus of NS4B (amino acid residues 229 to 253) that mediates membrane association and is involved in the formation of a functional HCV replication complex.
Mots-clé
Endoplasmic-Reticulum Membrane, Dependent Rna-Polymerase, Replication Complex, Binding Domain, Ns4b Protein, Identification, Determinants, Interfaces, Topology, Motif
Pubmed
Web of science
Open Access
Oui
Création de la notice
27/10/2009 15:35
Dernière modification de la notice
20/08/2019 15:11
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