4B1Q
NMR structure of the glycosylated conotoxin CcTx from Conus consors
Summary for 4B1Q
Entry DOI | 10.2210/pdb4b1q/pdb |
NMR Information | BMRB: 18897 |
Descriptor | CONOTOXIN CCTX, alpha-L-galactopyranose-(1-2)-beta-D-galactopyranose-(1-3)-[alpha-L-galactopyranose-(1-4)-2-acetamido-2-deoxy-alpha-D-glucopyranose-(1-6)]2-acetamido-2-deoxy-alpha-D-galactopyranose (2 entities in total) |
Functional Keywords | toxin, o-glycan |
Biological source | CONUS CONSORS |
Cellular location | Secreted: P58928 |
Total number of polymer chains | 1 |
Total formula weight | 4142.57 |
Authors | Hocking, H.G.,Gerwig, G.J.,Favreau, P.,Stocklin, R.,Kamerling, J.P.,Boelens, R. (deposition date: 2012-07-12, release date: 2013-02-06, Last modification date: 2025-04-09) |
Primary citation | Hocking, H.G.,Gerwig, G.J.,Dutertre, S.,Violette, A.,Favreau, P.,Stocklin, R.,Kamerling, J.P.,Boelens, R. Structure of the O-Glycosylated Conopeptide Cctx from Conus Consors Venom. Chemistry, 19:870-, 2013 Cited by PubMed 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. PubMed: 23281027DOI: 10.1002/CHEM.201202713 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
