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PROSITE documentation PDOC51200 |
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:
April 2006 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
1 | Authors | Lippens G. Najib J. Wodak S.J. Tartar A. |
Title | NMR sequential assignments and solution structure of chlorotoxin, a small scorpion toxin that blocks chloride channels. | |
Source | Biochemistry 34:13-21(1995). | |
PubMed ID | 7819188 |
2 | Authors | Adjadj E. Naudat V. Quiniou E. Wouters D. Sautiere P. Craescu C.T. |
Title | Solution structure of Lqh-8/6, a toxin-like peptide from a scorpion venom -- structural heterogeneity induced by proline cis/trans isomerization. | |
Source | Eur. J. Biochem. 246:218-227(1997). | |
PubMed ID | 9210487 |
3 | Authors | Ali S.A. Stoeva S. Schuetz J. Kayed R. Abassi A. Zaidi Z.H. Voelter W. |
Title | Purification and primary structure of low molecular mass peptides from scorpion (Buthus sindicus) venom. | |
Source | Comp. Biochem. Physiol. 121A:323-332(1998). | |
PubMed ID | 10048185 |