Structure of the Reston ebolavirus VP30 C-terminal domain

The ebolaviruses can cause severe hemorrhagic fever. Essential to the ebolavirus life cycle is the protein VP30, which serves as a transcriptional cofactor. Here, the crystal structure of the C-terminal, NP-binding domain of VP30 from Reston ebolavirus is presented. Reston VP30 and Ebola VP30 both f...

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Autores principales: Clifton, Matthew C., Kirchdoerfer, Robert N., Atkins, Kateri, Abendroth, Jan, Raymond, Amy, Grice, Rena, Barnes, Steve, Moen, Spencer, Lorimer, Don, Edwards, Thomas E., Myler, Peter J., Saphire, Erica Ollmann
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2014
Materias:
Structural Communications
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3976061/
https://www.ncbi.nlm.nih.gov/pubmed/24699737
http://dx.doi.org/10.1107/S2053230X14003811
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author Clifton, Matthew C.
Kirchdoerfer, Robert N.
Atkins, Kateri
Abendroth, Jan
Raymond, Amy
Grice, Rena
Barnes, Steve
Moen, Spencer
Lorimer, Don
Edwards, Thomas E.
Myler, Peter J.
Saphire, Erica Ollmann
author_facet Clifton, Matthew C.
Kirchdoerfer, Robert N.
Atkins, Kateri
Abendroth, Jan
Raymond, Amy
Grice, Rena
Barnes, Steve
Moen, Spencer
Lorimer, Don
Edwards, Thomas E.
Myler, Peter J.
Saphire, Erica Ollmann
author_sort Clifton, Matthew C.
collection PubMed
description The ebolaviruses can cause severe hemorrhagic fever. Essential to the ebolavirus life cycle is the protein VP30, which serves as a transcriptional cofactor. Here, the crystal structure of the C-terminal, NP-binding domain of VP30 from Reston ebolavirus is presented. Reston VP30 and Ebola VP30 both form homodimers, but the dimeric interfaces are rotated relative to each other, suggesting subtle inherent differences or flexibility in the dimeric interface.
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spelling pubmed-39760612014-04-24 Structure of the Reston ebolavirus VP30 C-terminal domain Clifton, Matthew C. Kirchdoerfer, Robert N. Atkins, Kateri Abendroth, Jan Raymond, Amy Grice, Rena Barnes, Steve Moen, Spencer Lorimer, Don Edwards, Thomas E. Myler, Peter J. Saphire, Erica Ollmann Acta Crystallogr F Struct Biol Commun Structural Communications The ebolaviruses can cause severe hemorrhagic fever. Essential to the ebolavirus life cycle is the protein VP30, which serves as a transcriptional cofactor. Here, the crystal structure of the C-terminal, NP-binding domain of VP30 from Reston ebolavirus is presented. Reston VP30 and Ebola VP30 both form homodimers, but the dimeric interfaces are rotated relative to each other, suggesting subtle inherent differences or flexibility in the dimeric interface. International Union of Crystallography 2014-03-25 /pmc/articles/PMC3976061/ /pubmed/24699737 http://dx.doi.org/10.1107/S2053230X14003811 Text en © Clifton et al. 2014 http://creativecommons.org/licenses/by/2.0/uk/ This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.
spellingShingle Structural Communications
Clifton, Matthew C.
Kirchdoerfer, Robert N.
Atkins, Kateri
Abendroth, Jan
Raymond, Amy
Grice, Rena
Barnes, Steve
Moen, Spencer
Lorimer, Don
Edwards, Thomas E.
Myler, Peter J.
Saphire, Erica Ollmann
Structure of the Reston ebolavirus VP30 C-terminal domain
title Structure of the Reston ebolavirus VP30 C-terminal domain
title_full Structure of the Reston ebolavirus VP30 C-terminal domain
title_fullStr Structure of the Reston ebolavirus VP30 C-terminal domain
title_full_unstemmed Structure of the Reston ebolavirus VP30 C-terminal domain
title_short Structure of the Reston ebolavirus VP30 C-terminal domain
title_sort structure of the reston ebolavirus vp30 c-terminal domain
topic Structural Communications
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3976061/
https://www.ncbi.nlm.nih.gov/pubmed/24699737
http://dx.doi.org/10.1107/S2053230X14003811
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