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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Cell Line
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Hepacivirus / metabolism*
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Humans
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Models, Molecular
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Molecular Sequence Data
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Protein Structure, Secondary*
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Protein Structure, Tertiary
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Recombinant Fusion Proteins / chemistry
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Recombinant Fusion Proteins / genetics
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Recombinant Fusion Proteins / metabolism
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Sequence Alignment
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Viral Nonstructural Proteins / chemistry*
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Viral Nonstructural Proteins / genetics
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Viral Nonstructural Proteins / metabolism
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Virus Internalization*
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Virus Replication
Substances
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Recombinant Fusion Proteins
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Viral Nonstructural Proteins