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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Detalles Bibliográficos
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
Descripción
Sumario: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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