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An amphipathic alpha-helix at the C terminus of hepatitis C virus nonstructural protein 4B mediates membrane association.
- Source :
-
Journal of virology [J Virol] 2009 Nov; Vol. 83 (21), pp. 11378-84. Date of Electronic Publication: 2009 Aug 19. - Publication Year :
- 2009
-
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.
- Subjects :
- Amino Acid Sequence
Cell Line
Humans
Models, Molecular
Molecular Sequence Data
Protein Structure, Tertiary
Recombinant Fusion Proteins chemistry
Recombinant Fusion Proteins genetics
Recombinant Fusion Proteins metabolism
Sequence Alignment
Viral Nonstructural Proteins genetics
Viral Nonstructural Proteins metabolism
Virus Replication
Hepacivirus metabolism
Protein Structure, Secondary
Viral Nonstructural Proteins chemistry
Virus Internalization
Subjects
Details
- Language :
- English
- ISSN :
- 1098-5514
- Volume :
- 83
- Issue :
- 21
- Database :
- MEDLINE
- Journal :
- Journal of virology
- Publication Type :
- Academic Journal
- Accession number :
- 19692468
- Full Text :
- https://doi.org/10.1128/JVI.01122-09