Perspectives in Drug Discovery and Design

, Volume 15, Issue 0, pp 15–40 | Cite as

Structure and function of scorpion toxins affecting K+-channels

  • Lourival D. Possani
  • Barbara Selisko
  • Georgina B. Gurrola


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.

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


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Copyright information

© Kluwer Academic Publishers 1999

Authors and Affiliations

  • Lourival D. Possani
    • 1
  • Barbara Selisko
    • 1
  • Georgina B. Gurrola
    • 1
  1. 1.Department of Molecular Recognition and Structural BiologyBiotechnology Institute – National Autonomous University of MexicoCuernavaca MORMexico

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