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Title: Evidence for a function-specific mutation in the neurotoxin, parabutoxin 3
Authors: Huys, Isabelle ×
Tytgat, Jan #
Issue Date: May-2003
Series Title: The European Journal of Neuroscience vol:17 issue:9 pages:1786-1792
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.
URI: 
ISSN: 0953-816X
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Toxicology and Pharmacology
Research Centre for Pharmaceutical Care and Pharmaco-economics (-)
Research Unit KU Leuven Centre for IT & IP Law (CiTiP)
× corresponding author
# (joint) last author

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