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2KDR

Solution structure of HCV NS4B(227-254)

Summary for 2KDR
Entry DOI10.2210/pdb2kdr/pdb
Related2JXF
NMR InformationBMRB: 16122
DescriptorNon-structural protein 4B (1 entity in total)
Functional Keywordshcv, ns4b, 227-254 segment, membranous web, replication complex, membrane, transmembrane, rna-binding, palmitate, viral protein, membrane protein
Biological sourceHepatitis C virus
Total number of polymer chains1
Total formula weight3111.60
Authors
Montserret, R.,Penin, F. (deposition date: 2009-01-15, release date: 2009-09-29, Last modification date: 2024-05-15)
Primary citationGouttenoire, J.,Montserret, R.,Kennel, A.,Penin, F.,Moradpour, D.
An amphipathic alpha-helix at the C terminus of hepatitis C virus nonstructural protein 4B mediates membrane association
J.Virol., 83:11378-11384, 2009
Cited by
PubMed 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.
PubMed: 19692468
DOI: 10.1128/JVI.01122-09
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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