PROSITE documentation PDOC51200
Scorpion short toxin chloride channel inhibitor subfamily profile


Short scorpion toxin chloride channel inhibitors are short-chain neurotoxins (SCNs) (see <PDOC00875>), which block small-conductance chloride channels. They are 30-40-residue long and contain four intramolecular disulfide bridges, which have been assigned as C1-C4, C2-C6, C3-C7 and C5-C8 [1,2,3].

The global fold of the scorpion short toxin chloride channel inhibitor subfamily is an α-helix packed on a two-stranded β-sheet (see <PDB:1CHL>). The structure also contains a short fragment in an extended form. The two antiparalllel β-strands are connected by a type I β-turn. The four disulfide bridges help to maintain a very compact structure by heavily attaching the N-terminal and C-terminal ends to the α-helix [1,2,3].

The scorpion short toxin chloride channel inhibitor subfamily includes:

  • Buthus sindicus chlorotoxin-like peptide Bs8 and Bs 14.
  • Mesobuthus martensii (Manchurian scorpion) short-chain Cl-channel toxin (BmKCT) and Neurotoxin Bm12-b from (Buthus martensii)
  • Buthus eupeus (Lesser Asian scorpion) insectotoxin BeI3, BeI4 and BeI5.
  • Parabuthus schlechteri (Scorpion) toxin PBITx1 (sITx10).
  • Leiurus quinquestriatus quinquestriatus (Egyptian scorpion) chlorotoxin (CTX).
  • Leiurus quinquestriatus hebraeus (Yellow scorpion) probable toxin Lqh-8/6.
  • Androctonus mauretanicus mauretanicus (Scorpion) neurotoxin P2.
Last update:

April 2006 / First entry.


Technical section

PROSITE method (with tools and information) covered by this documentation:

SHORT_SCORPION_CHLORIDE, PS51200; Scorpion short toxin chloride channel inhibitor subfamily profile  (MATRIX)


1AuthorsLippens G. Najib J. Wodak S.J. Tartar A.
TitleNMR sequential assignments and solution structure of chlorotoxin, a small scorpion toxin that blocks chloride channels.
SourceBiochemistry 34:13-21(1995).
PubMed ID7819188

2AuthorsAdjadj E. Naudat V. Quiniou E. Wouters D. Sautiere P. Craescu C.T.
TitleSolution structure of Lqh-8/6, a toxin-like peptide from a scorpion venom -- structural heterogeneity induced by proline cis/trans isomerization.
SourceEur. J. Biochem. 246:218-227(1997).
PubMed ID9210487

3AuthorsAli S.A. Stoeva S. Schuetz J. Kayed R. Abassi A. Zaidi Z.H. Voelter W.
TitlePurification and primary structure of low molecular mass peptides from scorpion (Buthus sindicus) venom.
SourceComp. Biochem. Physiol. 121A:323-332(1998).
PubMed ID10048185

PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.


View entry in original PROSITE document format
View entry in raw text format (no links)