Deduction of functional peptide motifs in scorpion toxins


Autoria(s): Tan, P. T. J.; Ranganathan, S.; Brusic, V.
Contribuinte(s)

J.R. Jones

Data(s)

01/01/2006

Resumo

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 (c) 2006 European Peptide Society and John Wiley & Sons, Ltd.

Identificador

http://espace.library.uq.edu.au/view/UQ:82853

Idioma(s)

eng

Publicador

John Wiley & Sons Ltd

Palavras-Chave #Biochemistry & Molecular Biology #Chemistry, Analytical #Scorpion Toxins #Binding Motifs #Mutation #Ion Channel Subtypes #Ca2+-activated K+ Channels #Alpha-like Toxin #Potassium Channels #Sodium-channels #Sequence Alignment #Tityus-serrulatus #Leiurotoxin-i #Animal Toxins #Na+ Channels #Binding-site #C1 #270103 Protein Targeting and Signal Transduction #670499 Other
Tipo

Journal Article