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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.

Original publication

DOI

10.1038/ncomms5874

Type

Journal article

Journal

Nat Commun

Publication Date

16/09/2014

Volume

5

Keywords

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