Deduction of functional peptide motifs in scorpion toxins
Copyright policy )Deduction of functional peptide motifs in scorpion toxins
AbstractScorpion 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. Copyright © 2006 European Peptide Society and John Wiley & Sons, Ltd.
- University of Queensland Australia
- Macquarie University Australia
- National University of Singapore Libraries Singapore
- National University of Singapore Singapore
- University of Queensland Australia
Biochemistry & Molecular Biology, Potassium Channels, Databases, Factual, Amino Acid Motifs, Molecular Sequence Data, Ion channel subtypes, 610, Scorpion Venoms, Binding-site, Binding, Competitive, Leiurotoxin-i, Protein Structure, Secondary, Sodium Channels, Scorpions, Structure-Activity Relationship, C1, 270103 Protein Targeting and Signal Transduction, 670499 Other, Chloride Channels, Animals, Ca2+-activated K+ Channels, Amino Acid Sequence, Na+ Channels, Sequence Homology, Amino Acid, Sodium-channels, Chemistry, Analytical, Animal Toxins, Binding motifs, Ion Channel Subtypes, Analytical, 540, Scorpion Toxins, Binding Motifs, Protein Structure, Tertiary, Scorpion toxins, Chemistry, Tityus-serrulatus, Alpha-like Toxin, Mutation, Kv1.1 Potassium Channel, Sequence Alignment
Biochemistry & Molecular Biology, Potassium Channels, Databases, Factual, Amino Acid Motifs, Molecular Sequence Data, Ion channel subtypes, 610, Scorpion Venoms, Binding-site, Binding, Competitive, Leiurotoxin-i, Protein Structure, Secondary, Sodium Channels, Scorpions, Structure-Activity Relationship, C1, 270103 Protein Targeting and Signal Transduction, 670499 Other, Chloride Channels, Animals, Ca2+-activated K+ Channels, Amino Acid Sequence, Na+ Channels, Sequence Homology, Amino Acid, Sodium-channels, Chemistry, Analytical, Animal Toxins, Binding motifs, Ion Channel Subtypes, Analytical, 540, Scorpion Toxins, Binding Motifs, Protein Structure, Tertiary, Scorpion toxins, Chemistry, Tityus-serrulatus, Alpha-like Toxin, Mutation, Kv1.1 Potassium Channel, Sequence Alignment
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