Origin of neurotoxins from defensins.
- Author:
Li-Mei ZHU
1
;
Bin GAO
1
;
Shun-Yi ZHU
2
Author Information
1. Group of Peptide Biology and Evolution, State Key Laboratory of Integrated Management of Pest Insects and Rodents, Institute of Zoology, Chinese Academy of Sciences, Beijing 100101, China.
2. Group of Peptide Biology and Evolution, State Key Laboratory of Integrated Management of Pest Insects and Rodents, Institute of Zoology, Chinese Academy of Sciences, Beijing 100101, China. zhusy@ioz.ac.cn.
- Publication Type:Journal Article
- MeSH:
Defensins;
chemistry;
Evolution, Molecular;
Neurotoxins;
chemistry;
Protein Structure, Secondary
- From:
Acta Physiologica Sinica
2015;67(3):239-247
- CountryChina
- Language:English
-
Abstract:
There are at least three conserved protein folds shared by ion channel-targeted neurotoxins and antimicrobial defensins, including cysteine-stabilized α-helix and β-sheet fold (CSαβ), inhibitor cystine knot fold (ICK) and β-defensin fold (BDF). Based on a combined data of sequences, structures and functions, it has been proposed that these neurotoxins could originate from related ancient antimicrobial defensins by neofunctionalization. This provides an ideal system to study how a novel function emerged from a conserved structural scaffold during evolution. The elucidation of functional novelty of proteins not only has great significance in evolutionary biology but also will be helpful in guiding rational molecular design. This review describes recent progresses in origin of neurotoxins, focusing on the three conserved protein scaffolds.
