1. Tc1, from Tityus cambridgei , is the first member of a new subfamily of scorpion toxin that blocks K+ -channels
- Author
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Lourival D. Possani, Froylan Gómez-Lagunas, Sylvia M. Lucas, and Cesar Vicente Ferreira Batista
- Subjects
Potassium Channels ,Subfamily ,Molecular Sequence Data ,Neurotoxins ,Biophysics ,Scorpion ,Scorpion Venoms ,Peptide ,Venom ,Spodoptera ,Tityus cambridgei ,complex mixtures ,Biochemistry ,Cell Line ,Scorpions ,Mice ,Structural Biology ,biology.animal ,Potassium Channel Blockers ,Genetics ,Animals ,Amino Acid Sequence ,Molecular Biology ,Peptide sequence ,chemistry.chemical_classification ,K+-channel ,Scorpion toxin ,biology ,Chemistry ,Cell Biology ,Amino acid ,Shaker Superfamily of Potassium Channels ,Peptides ,Synaptosomes - Abstract
A new peptide, Tc1, containing only 23 amino acids closely packed by three disulfide bridges was isolated from the Amazonian scorpion Tityus cambridgei. It blocks reversibly the Shaker B K+-channels with a Kd of 65 nM and displaces binding of noxiustoxin to mouse brain synaptosome membranes. It is the shortest known peptide from scorpion venom that recognizes K+-channels and constitutes a new structural subfamily of toxin, classified as alphaKTx 13.1.
- Published
- 2000
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