Toxin structures as evolutionary tools: Using conserved 3D folds to study the evolution of rapidly evolving peptides

Undheim, Eivind A., Mobli, Mehdi and King, Glenn F. (2016) Toxin structures as evolutionary tools: Using conserved 3D folds to study the evolution of rapidly evolving peptides. Bioessays, 38 6: 539-548. doi:10.1002/bies.201500165


Author Undheim, Eivind A.
Mobli, Mehdi
King, Glenn F.
Title Toxin structures as evolutionary tools: Using conserved 3D folds to study the evolution of rapidly evolving peptides
Journal name Bioessays   Check publisher's open access policy
ISSN 0265-9247
1521-1878
Publication date 2016-06-01
Year available 2016
Sub-type Critical review of research, literature review, critical commentary
DOI 10.1002/bies.201500165
Open Access Status Not yet assessed
Volume 38
Issue 6
Start page 539
End page 548
Total pages 10
Place of publication Chichester, West Sussex, United Kingdom
Publisher John Wiley & Sons
Language eng
Abstract Three-dimensional (3D) structures have been used to explore the evolution of proteins for decades, yet they have rarely been utilized to study the molecular evolution of peptides. Here, we highlight areas in which 3D structures can be particularly useful for studying the molecular evolution of peptide toxins. Although we focus our discussion on animal toxins, including one of the most widespread disulfide-rich peptide folds known, the inhibitor cystine knot, our conclusions should be widely applicable to studies of the evolution of disulfide-constrained peptides. We show that conserved 3D folds can be used to identify evolutionary links and test hypotheses regarding the evolutionary origin of peptides with extremely low sequence identity; construct accurate multiple sequence alignments; and better understand the evolutionary forces that drive the molecular evolution of peptides.
Formatted abstract
Three-dimensional (3D) structures have been used to explore the evolution of proteins for decades, yet they have rarely been utilized to study the molecular evolution of peptides. Here, we highlight areas in which 3D structures can be particularly useful for studying the molecular evolution of peptide toxins. Although we focus our discussion on animal toxins, including one of the most widespread disulfide-rich peptide folds known, the inhibitor cystine knot, our conclusions should be widely applicable to studies of the evolution of disulfide-constrained peptides. We show that conserved 3D folds can be used to identify evolutionary links and test hypotheses regarding the evolutionary origin of peptides with extremely low sequence identity; construct accurate multiple sequence alignments; and better understand the evolutionary forces that drive the molecular evolution of peptides.
Keyword Biochemistry & Molecular Biology
Biology
Biochemistry & Molecular Biology
Life Sciences & Biomedicine - Other Topics
Q-Index Code C1
Q-Index Status Provisional Code
Grant ID DP140101098
APP1072113
Institutional Status UQ

Document type: Journal Article
Sub-type: Critical review of research, literature review, critical commentary
Collections: HERDC Pre-Audit
Institute for Molecular Bioscience - Publications
Centre for Advanced Imaging Publications
 
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Citation counts: TR Web of Science Citation Count  Cited 7 times in Thomson Reuters Web of Science Article | Citations
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Created: Wed, 25 May 2016, 20:45:16 EST by Dr Mehdi Mobli on behalf of School of Chemistry & Molecular Biosciences