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J. Biol. Chem., Vol. 269, Issue 4, 2574-2580, Jan, 1994
M Fainzilber, O Kofman, E Zlotkin and D Gordon
The peptide conotoxin TxVIA is selectively toxic to molluscs and slows
sodium current inactivation in mollusc neurons. Here we show that TxVIA
binds with high affinity to new sites on sodium channels in both mollusc
and rat central nervous systems, despite its lack of toxicity to
vertebrates. Furthermore, TxVIA protects from the toxic effects of Conus
striatus toxin in rat brain. The TxVIA binding site differs from other
neurotoxin receptor sites affecting sodium channel inactivation in that
binding is not voltage-dependent and undergoes negative allosteric
modulation by veratridine. TxVIA therefore represents a novel category of
sodium channel probes, designated delta-conotoxins. TxVIA is shown to
discriminate between sodium channels in different phyla by activity but not
by binding, thus providing a lead for the study of structural elements
affecting gating modes of sodium channels.
A new neurotoxin receptor site on sodium channels is identified by a conotoxin that affects sodium channel inactivation in molluscs and acts as an antagonist in rat brain
Department of Cell and Animal Biology, Silberman Institute of Life Sciences, Hebrew University of Jerusalem, Israel.
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