Tc1, from Tityus cambridgei, is the first member of a new subfamily of scorpion toxin that blocks K(+)-channels

FEBS Lett. 2000 Dec 8;486(2):117-20. doi: 10.1016/s0014-5793(00)02253-5.

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 K(d) 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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cell Line
  • Mice
  • Molecular Sequence Data
  • Neurotoxins / classification
  • Neurotoxins / isolation & purification
  • Neurotoxins / metabolism*
  • Peptides / classification
  • Peptides / isolation & purification
  • Peptides / metabolism*
  • Potassium Channel Blockers*
  • Potassium Channels / genetics
  • Scorpion Venoms / classification
  • Scorpion Venoms / isolation & purification
  • Scorpion Venoms / metabolism*
  • Scorpions / metabolism*
  • Shaker Superfamily of Potassium Channels
  • Spodoptera / cytology
  • Synaptosomes / metabolism

Substances

  • Neurotoxins
  • Peptides
  • Potassium Channel Blockers
  • Potassium Channels
  • Scorpion Venoms
  • Shaker Superfamily of Potassium Channels
  • tityustoxin