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Crystal structure of the C-terminal domain of Ebola virus VP30 (strain Reston-89)Crystal structure of the C-terminal domain of Ebola virus VP30 (strain Reston-89)
Structural highlights
Publication Abstract from PubMedThe 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. Structure of the Reston ebolavirus VP30 C-terminal domain.,Clifton MC, Kirchdoerfer RN, Atkins K, Abendroth J, Raymond A, Grice R, Barnes S, Moen S, Lorimer D, Edwards TE, Myler PJ, Saphire EO Acta Crystallogr F Struct Biol Commun. 2014 Apr;70(Pt 4):457-60. doi:, 10.1107/S2053230X14003811. Epub 2014 Mar 25. PMID:24699737[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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