Ancient weapons: the three-dimensional structure of amoebapore A

Trends Parasitol. 2005 Jan;21(1):5-7. doi: 10.1016/


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.

Publication types

  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Dimerization
  • Entamoeba histolytica / metabolism*
  • Histidine / chemistry*
  • Ion Channels / chemistry*
  • Magnetic Resonance Spectroscopy
  • Protein Structure, Tertiary
  • Protozoan Proteins / chemistry*


  • Ion Channels
  • Protozoan Proteins
  • amoebapore proteins, protozoan
  • Histidine