HgeTx1, the first K+-channel specific toxin characterized from the venom of the scorpion Hadrurus gertschi Soleglad

Toxicon. 2006 Dec 15;48(8):1046-53. doi: 10.1016/j.toxicon.2006.08.009. Epub 2006 Sep 5.

Abstract

A novel toxin was identified, purified and characterized from the venom of the Mexican scorpion Hadrurus gertschi (abbreviated HgeTx1). It has a molecular mass of 3950 atomic mass units (a.m.u.) and contains 36 amino acids with four disulfide bridges established between Cys1-Cys5, Cys2-Cys6, Cys3-Cys7 and Cys4-Cys8. It blocks reversibly the Shaker B K(+)-channels with a Kd of 52nM. HgeTx1 shares 60%, 45% and 40% sequence identity, respectively, with Heterometrus spinnifer toxin1 (HsTX1), Scorpio maurus K(+)-toxin (maurotoxin) and Pandinus imperator toxin1 (Pi1), all four-disulfide bridged toxins. It is 57-58% identical with the other scorpion K(+)-channel toxins that contain only three disulfide bridges. Sequence comparison, chain length and number of disulfide bridges analysis classify HgeTx1 into subfamily 6 of the alpha-KTx scorpion toxins (systematic name: alpha-KTx 6.14).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cells, Cultured
  • Insecta / cytology
  • Molecular Sequence Data
  • Potassium Channel Blockers / chemistry*
  • Potassium Channel Blockers / isolation & purification
  • Scorpion Venoms / chemistry*
  • Scorpion Venoms / isolation & purification
  • Scorpions / chemistry
  • Sequence Alignment
  • Shaker Superfamily of Potassium Channels / antagonists & inhibitors*

Substances

  • Potassium Channel Blockers
  • Scorpion Venoms
  • Shaker Superfamily of Potassium Channels