A molluskivorous Conus toxin: conserved frameworks in conotoxins
- 10 January 1989
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 28 (1) , 358-361
- https://doi.org/10.1021/bi00427a049
Abstract
We purified and characterized a 27 amino acid toxin from a snail-hunting Conus venom, Conus textile. This toxin causes convulsive-like activity in snails and causes subordinate lobsters to assume an exaggerated dominant posture. The sequence of this peptide is Trp-Cys-Lys-Gln-Ser-Gly-Glu-Met-Cys-Asn-Leu-Leu-Asp-Gln-Asn-Cys-Cys-Asp-Gly-Tyr-Cys-Ile-Val-Leu-Val-Cys-Thr. The sequence was confirmed by determining the nucleotide sequence of a cDNA clone coding for the peptide. The conservation of Cys residues compared to the .omega.-conotoxins from piscivorous Conus venom suggests that toxins from different cone venoms may use only a few "Cys-motifs" as conserved structural backbones for targeting to a variety of receptors in different animals.This publication has 2 references indexed in Scilit:
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- Amino acid analysis by reverse-phase high-performance liquid chromatography: Precolumn derivatization with phenylisothiocyanateAnalytical Biochemistry, 1984