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Dipole moments of scorpion toxins direct the interaction towards small- or large-conductance Ca2+-activated K+ channels
Authors:Valé  rie Fré  mont, Eric Blanc, Marcel Crest, Marie-France Martin-Eauclaire, Maurice Gola, Hervé   Darbon  Jurphaas van Rietschoten
Affiliation:(1) CNRS UMR 6560, Laboratoire de Biochimie, Ingénierie des Protéines, Faculté de Médecine Nord, Boulevard Pierre Dramard, F-13916 Marseille Cédex 20, France;(2) CNRS UPR 9039, AFMB, Laboratoire de Neurobiologie, 31 Chemin Joseph Aiguier, F-13402 Marseille Cédex 20, France;(3) CNRS UPR 9024, Laboratoire de Neurobiologie, 31 Chemin Joseph Aiguier, F-13402 Marseille Cédex 20, France
Abstract:Ca2+-activated K+ channels consist of alarge family of membrane proteins, among which twogroups have been characterized by electrophysiologicalcriteria, the small conductance (SK) and the largeconductance (BK) Ca2+-activated K+channels. Scorpion toxins that block K+ channelsexhibit a common three-dimensional structureconstituted of a short agr-helix connected bydisulfide bonds to a beta-sheet. The leiurotoxin I(LTX1) related toxins interact specifically with theSK channel via basic residues of their agr-helix,while the charybdotoxin (ChTX) family recognizes theBK channel with basic residues of their beta-sheet.In an attempt to better understand thestructure–activity relationships of these toxins andthe characteristics of the electrostatic interactionswith the receptor site, we investigated theelectrostatic potential supported by natural toxinsand a synthetic analogue to find out if it may help inunderstanding the molecular mechanisms involved inthis peptide–protein interaction.
Keywords:Electrostatic interactions  Iberiotoxin  K+channel blockers  Leiurotoxin  Peptide-receptor interaction  Scorpion toxins
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