Structure of the Reston ebolavirus VP30 C‐terminal domain. Issue 4 (1st April 2014)

• Record Type: Journal Article
• Authors: 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
• Is Part Of: Acta crystallographica. Volume 70:Issue 4(2014:Apr.)
• Page Start: 457
• Page End: 460
• Publication Date: 2014-04-01
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X14003811
• Languages: English
• ISSNs: 2053-230X

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>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 <italic>Reston ebolavirus</italic> 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.</p> </abstract>