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Ancient weapons: the three-dimensional structure of amoebapore A
Matthias Leippe1, Heike Bruhn, Oliver Hecht
1Zoological Institute of the University of Kiel, Olshausenstr. 40, 24098 Kiel, Germany. mleippe@zoologie.uni-kiel.de
Abstract:
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.
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