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Sequence: [Cys3-Cys19, Cys6-Cys24, Cys10-Cys26]; H-Val-Ser-Cys3-Glu-Asp-Cys6-Pro-Asp-His-Cys10-Ser-Thr-Gln-Lys-Ala-Arg-Ala-Lys-Cys19-Asp-Asn-Asp-Lys-Cys24-Val-Cys26-Glu-Pro-Ile-OH
GaTx2 (gating modifier of anion channels 2) was isolated from the venom of Leiurus quinquestriatus hebraeus. GaTx2 is the most potent peptide inhibitor of ClC-2 chloride channel ever described. Kd value is close to 20 pM. GaTx2 slows ClC-2 activation but without altering channel conductance. The effect is voltage-dependent. It has no effect on ClC-0, ClC-1, ClC-3, ClC-4, CFTR, GABAC, Xenopus ClCa, Shaker B or Kv1.2 channels. Structurally, GaTx2 is composed of two ß-strands and one a-helix. This peptide is also called Leiuropeptide II. Bears 89, 93 and 96% identity with OdK1, neurotoxin PO1 and leiuropeptide III, respectively.