Deduction of functional peptide motifs in scorpion toxins | Macquarie University ResearchOnline

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Title: Deduction of functional peptide motifs in scorpion toxins
Related: Journal of peptide science, Vol. 12, Issue 6, p.420-427
DOI: 10.1002/psc.744
Publisher: John Wiley & Sons Ltd
Date: 2006
Author/Creator: Tan, Paul T. J
Author/Creator: Ranganathan, Shoba
Author/Creator: Brusic, Vladimir
Description: 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 structure-function relationship but are not normally used for extraction of binding motifs. 3D structure analyses also aid in the extraction of peptide motifs in which non-contiguous 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.
Description: 8 page(s)
Subject Keyword: scorpion toxins
Subject Keyword: binding motifs
Subject Keyword: mutation
Subject Keyword: ion channel subtypes
Resource Type: journal article
Organisation: Macquarie University. Dept. of Chemistry and Biomolecular Sciences

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