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


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.

SUBMITTER: El Omari K 

PROVIDER: S-EPMC4175578 | biostudies-literature | 2014 Sep

REPOSITORIES: biostudies-literature

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

El Omari Kamel K   Iourin Oleg O   Kadlec Jan J   Sutton Geoff G   Harlos Karl K   Grimes Jonathan M JM   Stuart David I DI  

Nature communications 20140916


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. ...[more]

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