A novel conotoxin, qc16a, with a unique cysteine framework and folding
Date
2011-04-15Author
Ye, Mingyu(Tongji Univ, Inst Prot Res)
Hong, Jing( Fuzhou Univ, Coll Biol Sci & Technol)
Zhou, Mi(Tongji Univ, Inst Prot Res)
Huang, Lijun(Tongji Univ, Inst Prot Res)
Shao, Xiaoxia(Tongji Univ, Inst Prot Res)
Yang, Youshan(Yale Univ, Sch Med)
Sigworth, Fred J.(Yale Univ, Sch Med)
Chi, Chengwu(Chinese Acad Sci, Shanghai Inst Biol Sci)
Lin, Donghai
林东海
Wang, Chunguang(Tongji Univ, Inst Prot Res)
Collections
- 化学化工-已发表论文 [14237]
Abstract
A novel conotoxin, qc16a, was identified from the venom of vermivorous Conus quercinus. qc16a has only 11 amino acid residues, DCQPCGHNVCC, with a unique cysteine pattern. Its disulfide connectivity was determined to be I-IV, II-III. The NMR structure shows that qc16a adopts a ribbon conformation with a simple beta-turn motif formed by residues Gly6, His7 and Asn8. qc16a causes depression symptom in mice when injected intracranially. Point mutation results showed that Asp1, His7 and Asn8 are all essential for the activity of qc16a. Electrophysiologically, qc16a has no strong effect on the whole-cell currents of neurons and the currents of Drosophila Shaker channels, human BK channels and Na(V)1.7 channels. Its specific target still remains to be identified. (C) 2011 Elsevier Inc. All rights reserved.
Citation
PEPTIDES,2011,32(6):1159-1165URI
http://dx.doi.org/doi:10.1016/j.peptides.2011.04.008WOS:000292586200010
https://dspace.xmu.edu.cn/handle/2288/11633
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