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- W2020320560 abstract "Parabutoxin 3 (PBTx3), a short-chain alpha-K+ neurotoxin from the scorpion, Parabuthus transvaalicus, is a 37-residue polypeptide cross-linked by three disulphide bridges. The affinity towards Kv1 channels is very weak (Kd approximately 79 micro m for Kv1.1 channels), or moderate (Kd approximately 500 nm for Kv1.2 and Kv1.3 channels). In an effort to generate a more potent K+ channel blocker, we recombinantly produced a mutant PBTx3 by the introduction of an aromatic amino acid, fenylalanine in close proximity of the crucial lysine 26 residue, to create a functional diad similar to subfamily three alpha-K+ toxins. The mutant was tested for his ability to block Kv1.1, Kv1.2 and Kv1.3 channels in Xenopus laevis oocytes: a hundred-fold higher affinity towards Kv1.1 channels and a fivefold increase in affinity towards Kv1.3 channels was observed, when compared to the wild-type toxin. The effect on Kv1.2 channels was similar to the wild-type toxin, indicating a specific interaction site for the mutated residue onto the different Kv-type channels." @default.
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- W2020320560 date "2003-05-01" @default.
- W2020320560 modified "2023-10-15" @default.
- W2020320560 title "Evidence for a function-specific mutation in the neurotoxin, parabutoxin 3" @default.
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- W2020320560 doi "https://doi.org/10.1046/j.1460-9568.2003.02613.x" @default.
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