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Precursor De13.1 from Conus delessertii defines the novel G gene superfamily.

Authors :
Aguilar MB
Ortiz E
Kaas Q
López-Vera E
Becerril B
Possani LD
de la Cotera EP
Source :
Peptides [Peptides] 2013 Mar; Vol. 41, pp. 17-20. Date of Electronic Publication: 2013 Jan 20.
Publication Year :
2013

Abstract

Peptide de13a was previously purified from the venom of the worm-hunting cone snail Conus delessertii from the Yucatán Channel, México. This peptide has eight cysteine (Cys) residues in the unique arrangement C-C-C-CC-C-C-C, which defines the cysteine framework XIII ("-" represents one or more non-Cys residues). Remarkably, δ-hydroxy-lysine residues have been found only in conotoxin de13a, which also contains an unusually high proportion of hydroxylated amino acid residues. Here, we report the cDNA cloning of the complete precursor De13.1 of a related peptide, de13b, which has the same Cys framework and inter-Cys spacings as peptide de13a, and shares high protein/nucleic acid sequence identity (87%/90%) with de13a, suggesting that both peptides belong to the same conotoxin gene superfamily. Analysis of the signal peptide of precursor De13.1 reveals that this precursor belongs to a novel conotoxin gene superfamily that we chose to name gene superfamily G. Thus far superfamily G only includes two peptides, each of which contains the same, distinctive Cys framework and a high proportion of amino acid residues with hydroxylated side chains.<br /> (Copyright © 2013 Elsevier Inc. All rights reserved.)

Details

Language :
English
ISSN :
1873-5169
Volume :
41
Database :
MEDLINE
Journal :
Peptides
Publication Type :
Academic Journal
Accession number :
23340018
Full Text :
https://doi.org/10.1016/j.peptides.2013.01.009