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Acta Crystallogr F Struct Biol Commun. 2014 Apr;70(Pt 4):457-60. doi: 10.1107/S2053230X14003811. Epub 2014 Mar 25.

Structure of the Reston ebolavirus VP30 C-terminal domain.

Author information

1
Seattle Structural Genomics Center for Infectious Disease (SSGCID), 307 Westlake Avenue North, Suite 500, Seattle, WA 98109, USA.
2
Department of Immunology and Microbial Science, The Scripps Research Institute, 10550 North Torrey Pines Road, IMM-21, La Jolla, CA 92037, USA.

Abstract

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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PMID:
24699737
PMCID:
PMC3976061
DOI:
10.1107/S2053230X14003811
[Indexed for MEDLINE]
Free PMC Article

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