Deduction of functional peptide motifs in scorpion toxins

Paul T.J. Tan, Shoba Ranganathan, Vladimir Brusic

Research output: Contribution to journalArticlepeer-review

11 Citations (Scopus)

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 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.

Original languageEnglish
Pages (from-to)420-427
Number of pages8
JournalJournal of Peptide Science
Volume12
Issue number6
DOIs
Publication statusPublished - Jun 1 2006

Keywords

  • Binding motifs
  • Ion channel subtypes
  • Mutation
  • Scorpion toxins

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Pharmacology
  • Drug Discovery
  • Organic Chemistry

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