Interaction of alpha-conotoxin ImII and its analogs with nicotinic receptors and acetylcholine-binding proteins: additional binding sites on Torpedo receptor

I.E. Kasheverov, M.N. Zhmak, A. Fish, P. Rucktooa, A.Y. Khruschov, A.V. Osipov, R.H. Ziganshin, D. D'Hoedt, D. Bertrand, T.K. Sixma, A.B. Smit, V.I. Tsetlin

Research output: Contribution to JournalArticleAcademicpeer-review

Abstract

α-Conotoxins interact with nicotinic acetylcholine receptors (nAChRs) and acetylcholine-binding proteins (AChBPs) at the sites for agonists/competitive antagonists. α-Conotoxins blocking muscle-type or α7 nAChRs compete with α-bungarotoxin. However, α-conotoxin ImII, a close homolog of the α7 nAChR-targeting α-conotoxin ImI, blocked α7 and muscle nAChRs without displacing α-bungarotoxin (Ellison et al. 2003, 2004), suggesting binding at a different site. We synthesized α-conotoxin ImII, its ribbon isomer (ImIIiso), 'mutant' ImII(W10Y) and found similar potencies in blocking human α7 and muscle nAChRs in Xenopus oocytes. Both isomers displaced [
Original languageEnglish
Pages (from-to)934-944
Number of pages10
JournalJournal of Neurochemistry
Volume111
DOIs
Publication statusPublished - 2009

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