Deduction of functional peptide motifs in scorpion toxins.
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.
Tan
Paul T J
PT
Institute for Infocomm Research, 21 Heng Mui Keng Terrace, Singapore 119613.
Ranganathan
Shoba
S
Brusic
Vladimir
V
D020816:Amino Acid Motifs / Q000235:genetics; D000595:Amino Acid Sequence; D000818:Animals; D001667:Binding, Competitive / Q000235:genetics; D018118:Chloride Channels / Q000737:chemistry / Q000378:metabolism; D016208:Databases, Factual; D051662:Kv1.1 Potassium Channel / Q000737:chemistry / Q000378:metabolism; D008969:Molecular Sequence Data; D009154:Mutation; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012604:Scorpion Venoms / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D012605:Scorpions / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D015222:Sodium Channels / Q000378:metabolism; D013329:Structure-Activity Relationship
D018118:Chloride Channels; D012604:Scorpion Venoms; D015222:Sodium Channels; D051662:Kv1.1 Potassium Channel