HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Cestèle, S. Articles by Gordon, D. Search for Related Content PubMed PubMed Citation Articles by Cestèle, S. Articles by Gordon, D. Social Bookmarking                      What's this?

Volume 271, Number 31, Issue of August 2, 1996 pp. 18329-18332
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

---

COMMUNICATION:
Tetrodotoxin Reverses Brevetoxin Allosteric Inhibition of Scorpion -Toxin Binding on Rat Brain Sodium Channels

(Received for publication, April 23, 1996, and in revised form, June 3, 1996)

From the Laboratory of Biochemistry, CNRS URA 1455, Faculty of Medicine Nord, Jean Roche Institute, Boulevard Pierre Dramard, 13916 Marseille Cedex 20, France

Voltage-sensitive sodium channels are responsible for the initiation of action potentials in many excitable cells. Several neurotoxins bind to distinct receptor sites on sodium channels and reveal strong allosteric interactions among them. Scorpion  toxins, which inhibit sodium channel inactivation by binding to receptor site 3, have been very important tools to study sodium channel structure and function. Recently, we have shown that brevetoxin induce a strong negative allosteric modulation on scorpion -toxin binding on rat brain sodium channels, in contrast to previously published studies. In this report we have examined the reasons for this discrepancy and found new, unexpected allosteric interactions between the tetrodotoxin and brevetoxin receptor sites, using scorpion -toxin as sensitive probe for subtle conformational changes on sodium channels. Tetrodotoxin reverses the negative modulation induced by brevetoxin on scorpion -toxin binding, revealing new dynamic interactions in sodium channel structure.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				F. V. Campos, B. Chanda, P. S.L. Beirao, and F. Bezanilla {alpha}-Scorpion Toxin Impairs a Conformational Change that Leads to Fast Inactivation of Muscle Sodium Channels J. Gen. Physiol., July 28, 2008; 132(2): 251 - 263. [Abstract] [Full Text] [PDF]

				L. Cohen, N. Lipstein, I. Karbat, N. Ilan, N. Gilles, R. Kahn, D. Gordon, and M. Gurevitz Miniaturization of Scorpion {beta}-Toxins Uncovers a Putative Ancestral Surface of Interaction with Voltage-gated Sodium Channels J. Biol. Chem., May 30, 2008; 283(22): 15169 - 15176. [Abstract] [Full Text] [PDF]

				A. Meir, S. Ginsburg, A. Butkevich, S. G. Kachalsky, I. Kaiserman, R. Ahdut, S. Demirgoren, and R. Rahamimoff Ion Channels in Presynaptic Nerve Terminals and Control of Transmitter Release Physiol Rev, July 1, 1999; 79(3): 1019 - 1088. [Abstract] [Full Text] [PDF]