Clifton MC¹, Kirchdoerfer RN², Atkins K¹, Abendroth J¹, Raymond A¹, Grice R¹, Barnes S¹, Moen S¹, Lorimer D¹, Edwards TE¹, Myler PJ¹, Saphire EO².

Author information

·         ¹Seattle Structural Genomics Center for Infectious Disease (SSGCID), 307 Westlake Avenue North, Suite 500, Seattle, WA 98109, USA.

·         ²Department 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 EbolaVP30 both form homodimers, but the dimeric interfaces are rotated relative to each other, suggesting subtle inherent differences or flexibility in the dimeric interface.

 下载全文：Structure of the Reston ebolavirus VP30 C-terminal domain.