Molecular determinants of binding of a wasp toxin (PMTXs) and its analogs in the Na+ channels proteins
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Data
2000-05-05
Autores
Konno, K.
Hisada, M.
Naoki, H.
Itagaki, Y.
Yasuhara, T.
Nakata, Y.
Miwa, A. K.
Kawai, N.
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Editor
Elsevier B.V.
Resumo
The structural specificity of alpha-PMTX, a novel peptide toxin derived from wasp venom has been studied on the neuromuscular synapse in the walking leg of the lobster. alpha-PMTX is known to induce repetitive action potentials in the presynaptic axon due to sodium channel inactivation. We synthesized 29 analogs of alpha-PMTX by substituting one or two amino acids and compared threshold concentrations of these mutant toxins for inducing repetitive action potentials. In 13 amino acid residues of alpha-PMTX, Arg-1, Lys-3 and Lys-12 regulate the toxic activity because substitution of these basic amino acid residues with other amino acid residues greatly changed the potency. Determining the structure-activity relationships of PMTXs will help clarifying the molecular mechanism of sodium channel inactivation. (C) 2000 Elsevier B.V. Ireland Ltd. All rights reserved.
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neurotoxin, sodium channel, inactivation, PMTX, neuromuscular synapse
Como citar
Neuroscience Letters. Clare: Elsevier Sci Ireland Ltd, v. 285, n. 1, p. 29-32, 2000.