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. 1988 Nov;85(22):8742-6.
doi: 10.1073/pnas.85.22.8742.

Site of covalent attachment of alpha-scorpion toxin derivatives in domain I of the sodium channel alpha subunit

F J Tejedor  1 , W A Catterall
Affiliations

Site of covalent attachment of alpha-scorpion toxin derivatives in domain I of the sodium channel alpha subunit

F J Tejedor et al. Proc Natl Acad Sci U S A. 1988 Nov.

Abstract

Purified and reconstituted sodium channels from rat brain have been photoaffinity labeled with a photoactivable derivative of the alpha-scorpion toxin V from Leiurus quinquestriatus (LqTx). A battery of sequence-specific antibodies has been used to determine which of the peptides produced by chemical and enzymatic cleavage of the photolabeled sodium-channel alpha subunit contain covalently attached LqTx. Nearly all of the covalently attached LqTx is found within homologous domain I. Two site-directed antisera, which recognize residues 317 to 335 and residues 382 to 400, respectively, specifically immunoprecipitate a 14-kDa peptide produced by CNBr digestion to which LqTx is covalently attached. It is proposed that a portion of the receptor site for alpha-scorpion toxins is formed by peptide segment(s) between amino acid residues 335 and 378 which is located in an extracellular loop between transmembrane helices S5 and S6 of homologous domain I of the sodium channel alpha subunit.

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