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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




Journal article


Nat Commun

Publication Date





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