Structural highlights
Function[CEX_CONCN] May specifically activate neuronal voltage-gated sodium channels (Nav) at the resting membrane potential. Causes a marked contraction and extension of the caudal and dorsal fins in fish and noticeable spontaneous contractions of isolated frog neuromuscular preparations. Publication Abstract from PubMedThe glycopeptide CcTx, isolated from the venom of the piscivorous cone snail Conus consors, belongs to the kappaA-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 kappaA-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 {alpha-L-Galp-(1-->4)-alpha-D-GlcpNAc-(1-->6)-[alpha-L-Galp-(1-->2)-beta-D-Galp-( 1-->3)-]alpha-D-GalpNAc-(1-->O)}, is highlighted. A sequence comparison to other putative members of the kappaA-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. Structure of the O-Glycosylated Conopeptide CcTx from Conus consors Venom.,Hocking HG, Gerwig GJ, Dutertre S, Violette A, Favreau P, Stocklin R, Kamerling JP, Boelens R Chemistry. 2013 Jan 14;19(3):870-9. doi: 10.1002/chem.201202713. Epub 2012 Dec, 27. PMID:23281027[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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