Structure of the Reston ebolavirus VP30 C-terminal domain.

Acta Crystallogr F Struct Biol Commun

Department of Immunology and Microbial Science, The Scripps Research Institute, 10550 North Torrey Pines Road, IMM-21, La Jolla, CA 92037, USA.

Published: April 2014

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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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3976061PMC
http://dx.doi.org/10.1107/S2053230X14003811DOI Listing

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