@article{ref1,
title="Structure of the O-Glycosylated Conopeptide CcTx from Conus consors Venom",
journal="Chemistry: a European journal",
year="2013",
author="Hocking, Henry G. and Gerwig, Gerrit J. and Dutertre, Sébastien and Violette, Aude and Favreau, Philipe and Stöcklin, Reto and Kamerling, Johannis P. and Boelens, Rolf",
volume="19",
number="3",
pages="870-879",
abstract="The glycopeptide CcTx, isolated from the venom of the piscivorous cone snail Conus consors, belongs to the κA-family of conopeptides. These toxins elicit excitotoxic responses in the prey by acting on voltage-gated sodium channels. The structure of CcTx, a first in the κA-family, has been determined by high-resolution NMR spectroscopy together with the analysis of its O-glycan at Ser7. A new type of glycopeptide O-glycan core structure, here registered as core type 9, containing two terminal L-galactose units {α-L-Galp-(1→4)-α-D-GlcpNAc-(1→6)-[α-L-Galp-(1→2)-β-D-Galp-(1→3)-]α-D-GalpNAc-(1→O)}, is highlighted. A sequence comparison to other putative members of the κA-family suggests that O-linked glycosylation might be more common than previously thought. This observation alone underlines the requirement for more careful and in-depth investigations into this type of post-translational modification in conotoxins.<p /><p>Language: en</p>",
language="en",
issn="0947-6539",
doi="10.1002/chem.201202713",
url="http://dx.doi.org/10.1002/chem.201202713"
}