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

Kamel El Omari, Oleg Iourin, Jan Kadlec, Geoff Sutton, Karl Harlos, Jonathan M. Grimes and David I. Stuart ()
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Kamel El Omari: The Wellcome Trust Centre for Human Genetics, University of Oxford, Headington, Oxford OX3 7BN, UK
Oleg Iourin: The Wellcome Trust Centre for Human Genetics, University of Oxford, Headington, Oxford OX3 7BN, UK
Jan Kadlec: The Wellcome Trust Centre for Human Genetics, University of Oxford, Headington, Oxford OX3 7BN, UK
Geoff Sutton: The Wellcome Trust Centre for Human Genetics, University of Oxford, Headington, Oxford OX3 7BN, UK
Karl Harlos: The Wellcome Trust Centre for Human Genetics, University of Oxford, Headington, Oxford OX3 7BN, UK
Jonathan M. Grimes: The Wellcome Trust Centre for Human Genetics, University of Oxford, Headington, Oxford OX3 7BN, UK
David I. Stuart: The Wellcome Trust Centre for Human Genetics, University of Oxford, Headington, Oxford OX3 7BN, UK

Nature Communications, 2014, vol. 5, issue 1, 1-5

Abstract: 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.

Date: 2014
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DOI: 10.1038/ncomms5874

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