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8.B.8 The α-KTx15 Scorpion Toxin (α-KTx15) Family

Discrepin is a scorpion peptide that blocks preferentially the I(A) currents of the voltage-dependent K(+) channel of rat cerebellum granular cells. It was isolated from the venom of the buthid scorpion Tityus discrepans and contains 38 amino acid residues with a pyroglutamic acid at the N-terminal site. Discrepin has the lowest sequence identity (approx. 50%) among the six members of the α-KTx15 sub-family of scorpion toxins (Romeo et al., 2008).

References associated with 8.B.8 family:

Huys, I., C.Q. Xu, C.Z. Wang, H. Vacher, M.F. Martin-Eauclaire, C.W. Chi, and J. Tytgat. (2004). BmTx3, a scorpion toxin with two putative functional faces separately active on A-type K+ and HERG currents. Biochem. J. 378: 745-752. 14599291
Prochnicka-Chalufour, A., G. Corzo, H. Satake, M.F. Martin-Eauclaire, A.R. Murgia, G. Prestipino, G. D'Suze, L.D. Possani, and M. Delepierre. (2006). Solution structure of discrepin, a new K+ -channel blocking peptide from the α- KTx15 subfamily. Biochemistry. 45: 1795-1804. 16460026
Romeo, S., G. Corzo, A. Vasile, H. Satake, G. Prestipino, and L.D. Possani. (2008). A positive charge at the N-terminal segment of Discrepin increases the blocking effect of K+ channels responsible for the I(A) currents in cerebellum granular cells. Biochim. Biophys. Acta. 1780: 750-755. 18280256