View source for 4b1q


==NMR structure of the glycosylated conotoxin CcTx from Conus consors==
<StructureSection load='4b1q' size='340' side='right'caption='[[4b1q]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4b1q]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Conus_consors Conus consors]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B1Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4B1Q FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A2G:N-ACETYL-2-DEOXY-2-AMINO-GALACTOSE'>A2G</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=GXL:ALPHA-L-GALACTOPYRANOSE'>GXL</scene>, <scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4b1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b1q OCA], [https://pdbe.org/4b1q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4b1q RCSB], [https://www.ebi.ac.uk/pdbsum/4b1q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4b1q ProSAT]</span></td></tr>
</table>
== Function ==
[[https://www.uniprot.org/uniprot/CEX_CONCN 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. 
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== Publication Abstract from PubMed ==
The 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--&gt;4)-alpha-D-GlcpNAc-(1--&gt;6)-[alpha-L-Galp-(1--&gt;2)-beta-D-Galp-( 1--&gt;3)-]alpha-D-GalpNAc-(1--&gt;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<ref>PMID:23281027</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Conus consors]]
[[Category: Large Structures]]
[[Category: Boelens, R]]
[[Category: Favreau, P]]
[[Category: Gerwig, G J]]
[[Category: Hocking, H G]]
[[Category: Kamerling, J P]]
[[Category: Stocklin, R]]
[[Category: O-glycan]]
[[Category: Toxin]]