Journal
TRENDS IN PARASITOLOGY
Volume 21, Issue 1, Pages 5-7Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.pt.2004.10.009
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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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