Structure and function of scorpion toxins affecting K+-channels

Abstract

This chapter reviews current literature dealing with peptides isolated from the venom of scorpions. Only peptides that recognize K+-channels are reported. They are called K+-channel-ligands or simply peptides, because the actual toxicity effects of all these peptides has not been demonstrated. The primary structures of 35 peptides are reviewed, and a general nomenclature has been proposed to define 9 distinct sub-families of related sequences. Partial sequences were not included in this classification. They are 29 to 39 amino acid residues long peptides with a common structural motif composed of an α-helix segment and three anti-parallel β-sheet strands stabilized by three or four disulfide bridges. Binding and/or electrophysiological experiments showed that the affinity of these peptides for the various sub-types of K+-channels varies from micromolar to picomolar concentrations. Some data on the three-dimensional structures and on specific functions of the various peptides on voltage-dependent K+-channels, high-conductance and small-conductance, Ca2+-dependent K+-channels are also briefly reviewed.

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Correspondence to Lourival D. Possani.

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Possani, L.D., Selisko, B. & Gurrola, G.B. Structure and function of scorpion toxins affecting K+-channels. Perspectives in Drug Discovery and Design 15, 15–40 (1999). https://doi.org/10.1023/A:1017062613503

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  • binding
  • K+-channels
  • nomenclature
  • peptide
  • scorpion toxins
  • three-dimensional structure
  • venom