| Title : Photoaffinity labeling of the receptor site for alpha-scorpion toxins on purified and reconstituted sodium channels by a new toxin derivative - Tejedor_1990_Cell.Mol.Neurobiol_10_257 |
| Author(s) : Tejedor FJ , Catterall WA |
| Ref : Cellular Molecular Neurobiology , 10 :257 , 1990 |
|
Abstract :
1. A methyl-4-azidobenzimidyl (MAB) derivative of the alpha-scorpion toxin from Leiurus quinquestriatus (LqTx) specifically labels only the alpha subunit of the rat brain sodium channel in synaptosomes or in purified and reconstituted sodium-channel preparations. 2. Unlike previous photoreactive toxin derivaties, binding and photolabeling by MAB-LqTx are allosterically modulated by tetrodotoxin and batrachotoxin, as observed for native LqTx binding to sodium channels in synaptosomes. 3. Proteolytic cleavage of the alpha subunit photolabeled with MAB-LqTx shows that the label is located within a 60 to 70-kDa protease-resistant core structure in domain I of the sodium-channel alpha subunit. 4. MAB-LqTx will be valuable in further defining the structure-activity relationships at the alpha-scorpion toxin receptor site. |
| PubMedSearch : Tejedor_1990_Cell.Mol.Neurobiol_10_257 |
| PubMedID: 2163754 |
Tejedor FJ, Catterall WA (1990)
Photoaffinity labeling of the receptor site for alpha-scorpion toxins on purified and reconstituted sodium channels by a new toxin derivative
Cellular Molecular Neurobiology
10 :257
Tejedor FJ, Catterall WA (1990)
Cellular Molecular Neurobiology
10 :257