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
Seattle Structural Genomics Center for Infectious Disease (SSGCID), 307 Westlake Avenue North, Suite 500, Seattle, WA 98109, USA.
Department of Immunology and Microbial Science, The Scripps Research Institute, 10550 North Torrey Pines Road, IMM-21, La Jolla, CA 92037, USA.
Acta Crystallogr F Struct Biol Commun. 2014 Apr;70(Pt 4):457-60. doi: 10.1107/S2053230X14003811. Epub 2014 Mar 25.
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.
埃博拉病毒可引发严重的出血热。对于埃博拉病毒的生命周期而言至关重要的是蛋白质VP30，它作为一种转录辅因子发挥作用。在此，展示了来自莱斯顿埃博拉病毒的VP30的C端NP结合结构域的晶体结构。莱斯顿VP30和埃博拉VP30均形成同型二聚体，但二聚体界面相对于彼此发生了旋转，这表明二聚体界面存在细微的内在差异或灵活性。
