期刊
BIOESSAYS
卷 38, 期 6, 页码 539-548出版社
WILEY
DOI: 10.1002/bies.201500165
关键词
inhibitor cystine knot; knottin; protein evolution; structural adaptation; toxin
资金
- Australian Research Council [DP140101098, FTI10100925, DE160101142]
- Australian National Health and Medical Research Council [APP1072113, APP1044414]
- Australian Research Council [DE160101142] Funding Source: Australian Research Council
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.
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