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


Autoria(s): Gouttenoire J.; Montserret R.; Kennel A.; Penin F.; Moradpour D.
Data(s)

2009

Resumo

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.

Identificador

http://serval.unil.ch/?id=serval:BIB_579AA3CFD580

isbn:1098-5514[electronic]

pmid:19692468

doi:10.1128/JVI.01122-09

isiid:000270602300050

Idioma(s)

en

Fonte

Journal of Virology, vol. 83, no. 21, pp. 11378-11384

Palavras-Chave #Endoplasmic-Reticulum Membrane; Dependent Rna-Polymerase; Replication Complex; Binding Domain; Ns4b Protein; Identification; Determinants; Interfaces; Topology; Motif
Tipo

info:eu-repo/semantics/article

article