ISSN:
1573-3904
Keywords:
Electrostatic interactions
;
Iberiotoxin
;
K+channel blockers
;
Leiurotoxin
;
Peptide-receptor interaction
;
Scorpion toxins
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
Notes:
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 α-helix connected bydisulfide bonds to a β-sheet. The leiurotoxin I(LTX1) related toxins interact specifically with theSK channel via basic residues of their α-helix,while the charybdotoxin (ChTX) family recognizes theBK channel with basic residues of their β-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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1023/A:1008892620231
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