title: An amphipathic alpha-helix at the C terminus of hepatitis C virus nonstructural protein 4B mediates membrane association.
abstract: 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.
authors.affiliation: Division of Gastroenterology and Hepatology, Centre Hospitalier Universitaire Vaudois, BU44/07/2421, Rue du Bugnon 44, CH-1011 Lausanne, Switzerland.
authors.forename: Jérôme
authors.initials: J
authors.lastname: Gouttenoire
authors.forename: Roland
authors.initials: R
authors.lastname: Montserret
authors.forename: Audrey
authors.initials: A
authors.lastname: Kennel
authors.forename: François
authors.initials: F
authors.lastname: Penin
authors.forename: Darius
authors.initials: D
authors.lastname: Moradpour
mesh_terms: D000595:Amino Acid Sequence; D002460:Cell Line; D016174:Hepacivirus / Q000378:metabolism*; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D016415:Sequence Alignment; D017361:Viral Nonstructural Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D053586:Virus Internalization; D014779:Virus Replication
chemical_list: D011993:Recombinant Fusion Proteins; D017361:Viral Nonstructural Proteins
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