Structural basis for Fullerene geometry in a human endogenous retrovirus capsid

In retroviruses, the capsid protein (CA) forms a shell surrounding the viral core. Here the authors combine cryo-electron microscopy with NMR and X-ray crystallography to examine the CA structure from the human endogenous retrovirus HML2 (HERV-K) and determine the structures of four Fullerene CA clo...

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Autores principales: Oliver Acton, Tim Grant, Giuseppe Nicastro, Neil J. Ball, David C. Goldstone, Laura E. Robertson, Kasim Sader, Andrea Nans, Andres Ramos, Jonathan P. Stoye, Ian A. Taylor, Peter B. Rosenthal
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Lenguaje:EN
Publicado: Nature Portfolio 2019
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Acceso en línea:https://doaj.org/article/50d5434d21c24069a587937d07c9ffa6
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spelling oai:doaj.org-article:50d5434d21c24069a587937d07c9ffa62021-12-02T17:01:32ZStructural basis for Fullerene geometry in a human endogenous retrovirus capsid10.1038/s41467-019-13786-y2041-1723https://doaj.org/article/50d5434d21c24069a587937d07c9ffa62019-12-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-13786-yhttps://doaj.org/toc/2041-1723In retroviruses, the capsid protein (CA) forms a shell surrounding the viral core. Here the authors combine cryo-electron microscopy with NMR and X-ray crystallography to examine the CA structure from the human endogenous retrovirus HML2 (HERV-K) and determine the structures of four Fullerene CA closed shells that reveal the molecular basis of capsid assembly.Oliver ActonTim GrantGiuseppe NicastroNeil J. BallDavid C. GoldstoneLaura E. RobertsonKasim SaderAndrea NansAndres RamosJonathan P. StoyeIan A. TaylorPeter B. RosenthalNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-13 (2019)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Oliver Acton
Tim Grant
Giuseppe Nicastro
Neil J. Ball
David C. Goldstone
Laura E. Robertson
Kasim Sader
Andrea Nans
Andres Ramos
Jonathan P. Stoye
Ian A. Taylor
Peter B. Rosenthal
Structural basis for Fullerene geometry in a human endogenous retrovirus capsid
description In retroviruses, the capsid protein (CA) forms a shell surrounding the viral core. Here the authors combine cryo-electron microscopy with NMR and X-ray crystallography to examine the CA structure from the human endogenous retrovirus HML2 (HERV-K) and determine the structures of four Fullerene CA closed shells that reveal the molecular basis of capsid assembly.
format article
author Oliver Acton
Tim Grant
Giuseppe Nicastro
Neil J. Ball
David C. Goldstone
Laura E. Robertson
Kasim Sader
Andrea Nans
Andres Ramos
Jonathan P. Stoye
Ian A. Taylor
Peter B. Rosenthal
author_facet Oliver Acton
Tim Grant
Giuseppe Nicastro
Neil J. Ball
David C. Goldstone
Laura E. Robertson
Kasim Sader
Andrea Nans
Andres Ramos
Jonathan P. Stoye
Ian A. Taylor
Peter B. Rosenthal
author_sort Oliver Acton
title Structural basis for Fullerene geometry in a human endogenous retrovirus capsid
title_short Structural basis for Fullerene geometry in a human endogenous retrovirus capsid
title_full Structural basis for Fullerene geometry in a human endogenous retrovirus capsid
title_fullStr Structural basis for Fullerene geometry in a human endogenous retrovirus capsid
title_full_unstemmed Structural basis for Fullerene geometry in a human endogenous retrovirus capsid
title_sort structural basis for fullerene geometry in a human endogenous retrovirus capsid
publisher Nature Portfolio
publishDate 2019
url https://doaj.org/article/50d5434d21c24069a587937d07c9ffa6
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