2KDR

Solution structure of HCV NS4B(227-254)

Summary for 2KDR

• Entry DOI: 10.2210/pdb2kdr/pdb
• Related: 2JXF
• NMR Information: BMRB: 16122
• Descriptor: Non-structural protein 4B (1 entity in total)
• Functional Keywords: hcv, ns4b, 227-254 segment, membranous web, replication complex, membrane, transmembrane, rna-binding, palmitate, viral protein, membrane protein
• Biological source: Hepatitis C virus
• Total number of polymer chains: 1
• Total formula weight: 3111.60

Authors

Montserret, R.,Penin, F. (deposition date: 2009-01-15, release date: 2009-09-29, Last modification date: 2024-05-15)

Primary citation

Gouttenoire, 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

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

Experimental method

SOLUTION NMR