7lqs: Difference between revisions

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'''Unreleased structure'''


The entry 7lqs is ON HOLD  until Paper Publication
==Structure of truncated conotoxin CIC==
<StructureSection load='7lqs' size='340' side='right'caption='[[7lqs]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7LQS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LQS FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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=7lqs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7lqs OCA], [https://pdbe.org/7lqs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7lqs RCSB], [https://www.ebi.ac.uk/pdbsum/7lqs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7lqs ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Cone snails are venomous marine predators that rely on fast-acting venom to subdue their prey and defend against aggressors. The conotoxins produced in the venom gland are small disulfide-rich peptides with high affinity and selectivity for their pharmacological targets. A dominant group comprises alpha-conotoxins, targeting nicotinic acetylcholine receptors. Here, we report on the synthesis, structure determination and biological activity of a novel alpha-conotoxin, CIC, found in the predatory venom of the piscivorous species Conus catus and its truncated mutant Delta-CIC. CIC is a 4/7 alpha-conotoxin with an unusual extended N-terminal tail. High-resolution NMR spectroscopy shows a major influence of the N-terminal tail on the apparent rigidity of the three-dimensional structure of CIC compared to the more flexible Delta-CIC. Surprisingly, this effect on the structure does not alter the biological activity, since both peptides selectively inhibit alpha3beta2 and alpha6/alpha3beta2beta3 nAChRs with almost identical sub- to low micromolar inhibition constants. Our results suggest that the N-terminal part of alpha-conotoxins can accommodate chemical modifications without affecting their pharmacology.


Authors: Evans, E.R.J., Daly, N.L.
Synthesis, Structural and Pharmacological Characterizations of CIC, a Novel alpha-Conotoxin with an Extended N-Terminal Tail.,Giribaldi J, Haufe Y, Evans ERJ, Wilson DT, Daly NL, Enjalbal C, Nicke A, Dutertre S Mar Drugs. 2021 Mar 2;19(3). pii: md19030141. doi: 10.3390/md19030141. PMID:33801301<ref>PMID:33801301</ref>


Description: Structure of truncated conotoxin CIC
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Evans, E.R.J]]
<div class="pdbe-citations 7lqs" style="background-color:#fffaf0;"></div>
[[Category: Daly, N.L]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Daly NL]]
[[Category: Evans ERJ]]
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