Dipole moments of scorpion toxins direct the interaction towards small- or large-conductance Ca2+-activated K+ channels |
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Authors: | Valé rie Fré mont, Eric Blanc, Marcel Crest, Marie-France Martin-Eauclaire, Maurice Gola, Hervé Darbon Jurphaas van Rietschoten |
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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 |
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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 -helix connected bydisulfide bonds to a -sheet. The leiurotoxin I(LTX1) related toxins interact specifically with theSK channel via basic residues of their -helix,while the charybdotoxin (ChTX) family recognizes theBK channel with basic residues of their -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. |
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Keywords: | Electrostatic interactions Iberiotoxin K+channel blockers Leiurotoxin Peptide-receptor interaction Scorpion toxins |
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