Leippe Matthias, Bruhn Heike, Hecht Oliver, Grötzinger Joachim
Zoological Institute of the University of Kiel, Olshausenstr. 40, 24098 Kiel, Germany.
Trends Parasitol. 2005 Jan;21(1):5-7. doi: 10.1016/j.pt.2004.10.009.
The recently solved three-dimensional structure of amoebapore A, the major pore-forming protein of Entamoeba histolytica, represents the first tertiary structure determined from a parasitic toxin. The implications derived from this solved structure, together with biochemical data, paint a picture of a unique activation mechanism and reveal that a histidine-mediated dimerization of the protein acts as the molecular switch for the formation of oligomeric pores in target cell membranes.
溶组织内阿米巴主要的成孔蛋白阿米巴穿孔素A最近解析出的三维结构,是首个从寄生性毒素中确定的三级结构。从这一解析出的结构以及生化数据中得出的结论描绘了一种独特的激活机制,表明该蛋白由组氨酸介导的二聚化作用充当了在靶细胞膜中形成寡聚孔的分子开关。