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An Amphipathic α-Helix at the C Terminus of Hepatitis C Virus Nonstructural Protein 4B Mediates Membrane Association
被引:49
|作者:
Gouttenoire, Jerome
[1
]
Montserret, Roland
[2
]
Kennel, Audrey
[1
]
Penin, Francois
[2
]
Moradpour, Darius
[1
]
机构:
[1] Univ Lausanne, CHU Vaudois, Div Gastroenterol & Hepatol, CH-1011 Lausanne, Switzerland
[2] Univ Lyon, CNRS, UMR 5086,Inst Biol & Chim Prot, IFR128 BioSci Gerland Lyon Sud, F-69367 Lyon, France
基金:
瑞士国家科学基金会;
关键词:
ENDOPLASMIC-RETICULUM MEMBRANE;
DEPENDENT RNA-POLYMERASE;
REPLICATION COMPLEX;
BINDING DOMAIN;
NS4B PROTEIN;
IDENTIFICATION;
DETERMINANTS;
INTERFACES;
TOPOLOGY;
MOTIF;
D O I:
10.1128/JVI.01122-09
中图分类号:
Q93 [微生物学];
学科分类号:
071005 ;
100705 ;
摘要:
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.
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页码:11378 / 11384
页数:7
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