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Deduction of functional peptide motifs in scorpion toxins
Author(s) -
Tan Paul T. J.,
Ranganathan Shoba,
Brusic Vladimir
Publication year - 2006
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.744
Subject(s) - scorpion , scorpion toxin , peptide , computational biology , function (biology) , scorpion venoms , structural motif , mutant , biology , chemistry , genetics , biochemistry , venom , gene
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. Copyright © 2006 European Peptide Society and John Wiley & Sons, Ltd.