Journal
NATURE COMMUNICATIONS
Volume 5, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/ncomms5874
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Funding
- Medical Research Council [G1000099]
- Wellcome Trust [075491/Z/04]
- MRC [G1000099, G19/3] Funding Source: UKRI
- Medical Research Council [G1000099, G19/3] Funding Source: researchfish
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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-angstrom 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.
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