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

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 co...

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Detalles Bibliográficos
Autores principales: El Omari, Kamel, Iourin, Oleg, Kadlec, Jan, Sutton, Geoff, Harlos, Karl, Grimes, Jonathan M., Stuart, David I.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Pub. Group 2014
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4175578/
https://www.ncbi.nlm.nih.gov/pubmed/25224686
http://dx.doi.org/10.1038/ncomms5874
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author El Omari, Kamel
Iourin, Oleg
Kadlec, Jan
Sutton, Geoff
Harlos, Karl
Grimes, Jonathan M.
Stuart, David I.
author_facet El Omari, Kamel
Iourin, Oleg
Kadlec, Jan
Sutton, Geoff
Harlos, Karl
Grimes, Jonathan M.
Stuart, David I.
author_sort El Omari, Kamel
collection PubMed
description 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.
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spelling pubmed-41755782014-10-02 Unexpected structure for the N-terminal domain of hepatitis C virus envelope glycoprotein E1 El Omari, Kamel Iourin, Oleg Kadlec, Jan Sutton, Geoff Harlos, Karl Grimes, Jonathan M. Stuart, David I. Nat Commun Article 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. Nature Pub. Group 2014-09-16 /pmc/articles/PMC4175578/ /pubmed/25224686 http://dx.doi.org/10.1038/ncomms5874 Text en Copyright © 2014, Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved. http://creativecommons.org/licenses/by/4.0/ 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. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
spellingShingle Article
El Omari, Kamel
Iourin, Oleg
Kadlec, Jan
Sutton, Geoff
Harlos, Karl
Grimes, Jonathan M.
Stuart, David I.
Unexpected structure for the N-terminal domain of hepatitis C virus envelope glycoprotein E1
title Unexpected structure for the N-terminal domain of hepatitis C virus envelope glycoprotein E1
title_full Unexpected structure for the N-terminal domain of hepatitis C virus envelope glycoprotein E1
title_fullStr Unexpected structure for the N-terminal domain of hepatitis C virus envelope glycoprotein E1
title_full_unstemmed Unexpected structure for the N-terminal domain of hepatitis C virus envelope glycoprotein E1
title_short Unexpected structure for the N-terminal domain of hepatitis C virus envelope glycoprotein E1
title_sort unexpected structure for the n-terminal domain of hepatitis c virus envelope glycoprotein e1
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4175578/
https://www.ncbi.nlm.nih.gov/pubmed/25224686
http://dx.doi.org/10.1038/ncomms5874
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