The structural basis of paramyxovirus invasion

To deliver their genetic material into host cells, enveloped viruses have surface glycoproteins that actively cause the fusion of the viral and cellular membranes. Recently determined X-ray crystal structures of the paramyxovirus fusion (F) protein in its pre-fusion and post-fusion conformations rev...

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Detalles Bibliográficos
Autores principales: Russell, Charles J., Luque, Laura E.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier Ltd. 2006
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7119026/
https://www.ncbi.nlm.nih.gov/pubmed/16678421
http://dx.doi.org/10.1016/j.tim.2006.04.004
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author Russell, Charles J.
Luque, Laura E.
author_facet Russell, Charles J.
Luque, Laura E.
author_sort Russell, Charles J.
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description To deliver their genetic material into host cells, enveloped viruses have surface glycoproteins that actively cause the fusion of the viral and cellular membranes. Recently determined X-ray crystal structures of the paramyxovirus fusion (F) protein in its pre-fusion and post-fusion conformations reveal the dramatic structural transformation that this protein undergoes while causing membrane fusion. Conformational changes in key regions of the F protein suggest the mechanism by which the F protein is activated and refolds.
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spelling pubmed-71190262020-04-03 The structural basis of paramyxovirus invasion Russell, Charles J. Luque, Laura E. Trends Microbiol Article To deliver their genetic material into host cells, enveloped viruses have surface glycoproteins that actively cause the fusion of the viral and cellular membranes. Recently determined X-ray crystal structures of the paramyxovirus fusion (F) protein in its pre-fusion and post-fusion conformations reveal the dramatic structural transformation that this protein undergoes while causing membrane fusion. Conformational changes in key regions of the F protein suggest the mechanism by which the F protein is activated and refolds. Elsevier Ltd. 2006-06 2006-05-04 /pmc/articles/PMC7119026/ /pubmed/16678421 http://dx.doi.org/10.1016/j.tim.2006.04.004 Text en Copyright © 2006 Elsevier Ltd. All rights reserved. Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.
spellingShingle Article
Russell, Charles J.
Luque, Laura E.
The structural basis of paramyxovirus invasion
title The structural basis of paramyxovirus invasion
title_full The structural basis of paramyxovirus invasion
title_fullStr The structural basis of paramyxovirus invasion
title_full_unstemmed The structural basis of paramyxovirus invasion
title_short The structural basis of paramyxovirus invasion
title_sort structural basis of paramyxovirus invasion
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7119026/
https://www.ncbi.nlm.nih.gov/pubmed/16678421
http://dx.doi.org/10.1016/j.tim.2006.04.004
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