Scyllatoxin
From Wikipedia, the free encyclopedia
 |
This article may require cleanup to meet Wikipedia's quality standards. Please discuss this issue on the talk page or replace this tag with a more specific message. This article has been tagged since November 2006. |
Scyllatoxin is a toxin from the scorpion Leiurus quinquestriatus hebraeus, which blocks small-conductance Ca2+-activated K+ channels.
Contents |
[edit] Source
Scyllatoxin (also leiurotoxin I) is one of the components of the venom of the Israeli scorpion ‘Leiurus quinquestriatus hebraeus’. It consists of only 0.02% of the total protein in crude venom. [1]
[edit] Chemistry
Leiurotoxin I is a 31-residue toxin, with a helix and a short antiparallel β-sheet. This toxin is stabilized by disulfide bonds: Cys8-Cys26 and Cys12-Cys28 is bound to the ß-sheet, Cys3-Cys21 is bound to an N-terminal segment preceding the helix. Leiurotoxin adopts the ά/β motif. [1] Especially the positively charged residues (Arg6 and Arg13, which are located in the ά helix) are important for the expression of toxin biological activities[2] and for its receptor affinity. [3]
[edit] Target
Scyllatoxin is a blocker of small-conductance Ca2+– activated K+ channels at 10-13 – 10-11 M concentrations in various cell types. [1] This toxin shows similarity in its physiological activity and binding specificity to apamin [1], but both toxins show no structural similarity. [4]
[edit] Mode of action
Scyllatoxin blocks the slow after-hyperpolarization that follows an action potential in some nerve cells. [1]
[edit] Toxicity
Scyllatoxin induces spontaneous contractions in guinea pig taenia coli muscle cells that have been relaxed with epinephrine. [5]
[edit] Treatment
 |
This section is a stub. You can help by expanding it. |
[edit] References
- ^ a b c d e Zhu Q., Liang S., Martin L., Gasparini S., Me´nez A., Vita C..Role of Disulfide Bonds in Folding and Activity of Leiurotoxin I: Just Two Disulfides Suffice. Biochemistry 2002; 41: 11488-11494.
- ^ Sabatier J.M., Lecomte C., Mabrouk K., Darbon H., Oughideni R., Canarelli S., Rochat H., Martin-Eauclaire M.F., Van Rietschoten J. Synthesis and Characterization of Leiurotoxin I Analogs Lacking One Disulfide Bridge: Evidence That Disulfide Pairing 3-21 Is Not Required for Full Toxin Activity. Biochemistry 1996; 35: 10641-10647.
- ^ Buisine E. Wieruszeski J.M., Lippens G., Wouters D., Tartar A., Sautiere P. Characterization of a new family of toxin-like peptides from the venom of the scorpion Leiurus quinquestriatus hebraeus. 1H-NMR structure of leiuropeptide II. J. Pept. Res. 1997;49:545-55
- ^ Chicchi G.G., Gimenez-Gallego G., Ber E. Garcia M.L. Winquist R. Cascieri M.A. Purification and characterization of a unique, potent inhibitor of apamin binding from Leiurus quinquestriatus hebraeus venom. J. Biol. Chem. 1988; 21: 10192-7.
- ^ Auguste P., Hugues M., Mourre C., Moinier D., Tartar A., Lazdunski M.. Scyllatoxin, a Blocker of Ca2+-Activated K+ Channels: Structure-Function Relationships and Brain Localization of the Binding Sites. Biochemistry 1992; 31:648-654.
