{PDOC51200} {PS51200; SHORT_SCORPION_CHLORIDE} {BEGIN} ********************************************************************* * Scorpion short toxin chloride channel inhibitor subfamily profile * ********************************************************************* Short scorpion toxin chloride channel inhibitors are short-chain neurotoxins (SCNs) (see ), 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 [1-3]. The global fold of the scorpion short toxin chloride channel inhibitor subfamily is an alpha-helix packed on a two-stranded beta-sheet (see ). The structure also contains a short fragment in an extended form. The two antiparalllel beta-strands are connected by a type I beta-turn. The four disulfide bridges help to maintain a very compact structure by heavily attaching the N-terminal and C-terminal ends to the alpha-helix [1-3]. 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. -Sequences known to belong to this class detected by the profile: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Last update: April 2006 / First entry. [ 1] Lippens G., Najib J., Wodak S.J., Tartar A. "NMR sequential assignments and solution structure of chlorotoxin, a small scorpion toxin that blocks chloride channels." Biochemistry 34:13-21(1995). PubMed=7819188 [ 2] Adjadj E., Naudat V., Quiniou E., Wouters D., Sautiere P., Craescu C.T. "Solution structure of Lqh-8/6, a toxin-like peptide from a scorpion venom -- structural heterogeneity induced by proline cis/trans isomerization." Eur. J. Biochem. 246:218-227(1997). PubMed=9210487 [ 3] Ali S.A., Stoeva S., Schuetz J., Kayed R., Abassi A., Zaidi Z.H., Voelter W. "Purification and primary structure of low molecular mass peptides from scorpion (Buthus sindicus) venom." Comp. Biochem. Physiol. 121A:323-332(1998). PubMed=10048185 -------------------------------------------------------------------------------- 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 https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}