The Pandinotoxins, PiTX-Kβ£ and PiTX-Kβ€, are members of the Charybdotoxin family of scorpion toxins that can be used to characterize K Ψ channels. PiTX-Kβ£ differs from PiTX-Kβ€, another peptide from Pandinus imperator, by one residue (P10E). When the two toxins are compared in a physiological assay,
Deduction of functional peptide motifs in scorpion toxins
β Scribed by Paul T. J. Tan; Shoba Ranganathan; Vladimir Brusic
- Publisher
- John Wiley and Sons
- Year
- 2006
- Tongue
- English
- Weight
- 163 KB
- Volume
- 12
- Category
- Article
- ISSN
- 1075-2617
- DOI
- 10.1002/psc.744
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β¦ Synopsis
Abstract
Scorpion toxins are important physiological probes for characterizing ion channels. Molecular databases have limited functional annotation of scorpion toxins. Their function can be inferred by searching for conserved motifs in sequence signature databases that are derived statistically but are not necessarily biologically relevant. Mutation studies provide biological information on residues and positions important for structureβfunction relationship but are not normally used for extraction of binding motifs. 3D structure analyses also aid in the extraction of peptide motifs in which nonβcontiguous residues are clustered spatially. Here we present new, functionally relevant peptide motifs for ion channels, derived from the analyses of scorpion toxin native and mutant peptides. Copyright Β© 2006 European Peptide Society and John Wiley & Sons, Ltd.
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## Abstract Using GFP as a reporter gene, splicing of scorpion toxin gene BmKK2 was investigated in cultured HEK 293T cells. The results of RTβPCR and western blotting showed that BmKK2's intron could be recognized and spliced in cultured HEK 293T cells. At the same time, a cryptic splicing site of