Lingel Andreas, Simon Bernd, Izaurralde Elisa, Sattler Michael
European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany.
EMBO Rep. 2005 Dec;6(12):1149-55. doi: 10.1038/sj.embor.7400583.
We report the structure of the flock house virus B2 protein, a potent suppressor of RNA interference (RNAi) in animals and plants. The B2 protein is a homodimer in solution and contains three alpha-helices per monomer. Chemical shift perturbation shows that an antiparallel arrangement of helices (alpha2/alpha2') forms an elongated binding interface with double-stranded RNA (dsRNA). This implies a novel mode of dsRNA recognition and provides insights into the mechanism of RNAi suppression by B2.
我们报道了禽舍病毒B2蛋白的结构，该蛋白是动植物中RNA干扰（RNAi）的有效抑制剂。B2蛋白在溶液中为同型二聚体，每个单体包含三个α螺旋。化学位移扰动表明，螺旋（α2/α2'）的反平行排列与双链RNA（dsRNA）形成了一个细长的结合界面。这暗示了一种新的dsRNA识别模式，并为B2抑制RNAi的机制提供了见解。
