Journal article
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.
- Publication status:
- Published
- Peer review status:
- Peer reviewed
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(Preview, Version of record, pdf, 831.8KB, Terms of use)
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- Publisher copy:
- 10.1038/ncomms5874
Authors
- Publisher:
- Springer Nature
- Journal:
- Nature Communications More from this journal
- Volume:
- 5
- Article number:
- 4874
- Publication date:
- 2014-09-16
- Acceptance date:
- 2014-07-31
- DOI:
- EISSN:
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2041-1723
- Language:
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English
- Keywords:
- UUID:
-
uuid:1a7856cf-2526-4512-8c42-25f0a17dbf74
- Local pid:
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pubs:484792
- Source identifiers:
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484792
- Deposit date:
-
2014-10-07
Terms of use
- Copyright holder:
- Macmillan Publishers Limited
- Copyright date:
- 2014
- Notes:
- © 2014 Macmillan Publishers Limited. All rights reserved. This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material.
- Licence:
- CC Attribution (CC BY)
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