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Sequence: [Cys8-Cys28, Cys14-Cys33, Cys18-Cys35]; H-Gly-Val-Glu-Ile-Asn-Val-Lys-Cys-Ser-Gly-Ser-Pro-Gln-Cys-Leu-Lys-Pro-Cys-Lys-Asp-Ala-Gly-Met-Arg-Phe-Gly-Lys-Cys-Met-Asn-Arg-Lys-Cys-His-Cys-Thr-Pro-Lys-NH2
Kaliotoxin-1 has been isolated from the venom of the Scorpion Androctonus mauretanicus mauretanicus. Kaliotoxin-1 is a potent inhibitor of large conductance calcium-activated potassium channels (BK-Ca). This toxin also binds to the dendrotoxin sensitive voltage-dependent potassium channel. It appears to block channel activity by a simple bimolecular inhibition process. Kaliotoxin-1 induces a transient period of fast flickering in the channel openings, followed by an almost complete blockade of the channel. Its binding affinity to rat brain synaptosomes is 5-fold higher than this of KTX-3. Binding of the toxin to the channel is associated with significant structural rearrangments in both molecules.