8f04: Difference between revisions

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'''Unreleased structure'''


The entry 8f04 is ON HOLD  until Paper Publication
==Structure of elevenin-Vc1 from venom of the Australian cone snail Conus victoriae==
<StructureSection load='8f04' size='340' side='right'caption='[[8f04]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8f04]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Conus_victoriae Conus victoriae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8F04 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8F04 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=8f04 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8f04 OCA], [https://pdbe.org/8f04 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8f04 RCSB], [https://www.ebi.ac.uk/pdbsum/8f04 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8f04 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CELE_CONVC CELE_CONVC] May mimic the function of prey elevenin neuropeptide. In vivo, intracranial injection in mice induces hyperactivity (tested at 5 and 10 nM).<ref>PMID:36827123</ref>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Elevenins are peptides found in a range of organisms, including arthropods, annelids, nematodes, and molluscs. They consist of 17 to 19 amino acid residues with a single conserved disulfide bond. The subject of this study, elevenin-Vc1, was first identified in the venom of the cone snail Conus victoriae (Gen. Comp. Endocrinol. 2017, 244, 11-18). Although numerous elevenin sequences have been reported, their physiological function is unclear, and no structural information is available. Upon intracranial injection in mice, elevenin-Vc1 induced hyperactivity at doses of 5 or 10 nmol. The structure of elevenin-Vc1, determined using nuclear magnetic resonance spectroscopy, consists of a short helix and a bend region stabilised by the single disulfide bond. The elevenin-Vc1 structural fold is similar to that of alpha-conotoxins such as alpha-RgIA and alpha-ImI, which are also found in the venoms of cone snails and are antagonists at specific subtypes of nicotinic acetylcholine receptors (nAChRs). In an attempt to mimic the functional motif, Asp-Pro-Arg, of alpha-RgIA and alpha-ImI, we synthesised an analogue, designated elevenin-Vc1-DPR. However, neither elevenin-Vc1 nor the analogue was active at six different human nAChR subtypes (alpha1beta1epsilondelta, alpha3beta2, alpha3beta4, alpha4beta2, alpha7, and alpha9alpha10) at 1 microM concentrations.


Authors:  
Characterisation of Elevenin-Vc1 from the Venom of Conus victoriae: A Structural Analogue of alpha-Conotoxins.,Krishnarjuna B, Sunanda P, Seow J, Tae HS, Robinson SD, Belgi A, Robinson AJ, Safavi-Hemami H, Adams DJ, Norton RS Mar Drugs. 2023 Jan 25;21(2):81. doi: 10.3390/md21020081. PMID:36827123<ref>PMID:36827123</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 8f04" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Conus victoriae]]
[[Category: Large Structures]]
[[Category: Krishnarjuna B]]
[[Category: Norton RS]]
[[Category: Sunanda P]]

Latest revision as of 14:32, 6 November 2024

Structure of elevenin-Vc1 from venom of the Australian cone snail Conus victoriae

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