Unexpected structure for the N-terminal domain of hepatitis C virus envelope glycoprotein E1

Nat Commun. 2014 Sep 16:5:4874. doi: 10.1038/ncomms5874.

Abstract

Hepatitis C virus (HCV) infection remains a major health problem worldwide. HCV entry into host cells and membrane fusion are achieved by two envelope glycoproteins, E1 and E2. We report here the 3.5-Å resolution crystal structure of the N-terminal domain of the HCV E1 ectodomain, which reveals a complex network of covalently linked intertwined homodimers that do not harbour the expected truncated class II fusion protein fold.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Crystallography, X-Ray
  • Gene Expression
  • HEK293 Cells
  • Hepacivirus / chemistry*
  • Humans
  • Molecular Sequence Data
  • Protein Folding
  • Protein Multimerization
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Viral Envelope Proteins / chemistry*
  • Viral Envelope Proteins / genetics

Substances

  • E1 protein, Hepatitis C virus
  • Recombinant Proteins
  • Viral Envelope Proteins

Associated data

  • PDB/4UOI