Kurtoxin

Amino Acid Sequence

Lys-Ile-Asp-Gly-Tyr-Pro-Val-Asp-Tyr-Trp-Asn-Cys-Lys-Arg-Ile-Cys-Trp-Tyr-Asn-Asn-Lys-Tyr-Cys-Asn-Asp-Leu-Cys-Lys-Gly-Leu-Lys-Ala-Asp-Ser-Gly-Tyr-Cys-Trp-Gly-Trp-Thr-Leu-Ser-Cys-Tyr-Cys-Gln-Gly-Leu-Pro-Asp-Asn-Ala-Arg-Ile-Lys-Arg-Ser-Gly-Arg-Cys-Arg-Ala

General description

Kurtoxin is hydrophobic in nature and shares sequence identity with α-scorpion and has cysteine-stabilized α-helix and β-sheet (CSαβ) motif. It interacts with N-type, and P-type calcium (Ca²⁺) channels as well.

Application

Kurtoxin has been used as a blocker of T-type and R-Type voltage-gated calcium channels (VGGCs) in hippocampal neurons.

Biochem/physiol Actions

Kurtoxin is isolated from the venom of the South African scorpion Parabuthus transvaalicus. It associates with voltage-gated sodium channels and delays their inactivation.

T-type Ca²⁺ channel blocker; Scorpion toxin