期刊
PEPTIDES
卷 29, 期 9, 页码 1521-1525出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/j.peptides.2008.05.015
关键词
conotoxin; cysteine framework; signal peptide
资金
- National Basic Research Program of China [2004CB719900]
- Initiation Funding of Tongji University [2000144005]
A new conotoxin, ca16a, containing 8 cysteine residues was purified, sequenced, and cloned from a worm-hunting snail, Conus caracteristicus. This conotoxin is an extremely hydrophilic peptide comprising 34 residues, with 4 acidic and 4 basic residues. it is rich in polar Gly, Ser, and Thr residues and includes a hydroxylated Pro residue. The cysteine arrangement pattern of ca16a (-C-C-CC-C-CC-C-, designated as framework #16) is distinct from that of other known conotoxins. Furthermore, the signal peptide sequence of this conotoxin does not share any homology with those of other conotoxins. Leu residues account for almost 50% of its 20-residue signal peptide. The unique cysteine framework and signal peptide sequence of ca16a suggest that it belongs to a new conotoxin superfamily. (C) 2008 Elsevier Inc. All rights reserved.
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