View source for 8pwt


==Solution structure of the peptide U11-MYRTX-Tb1a from the venom of the ant Tetramorium bicarinatum==
<StructureSection load='8pwt' size='340' side='right'caption='[[8pwt]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8pwt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Tetramorium_bicarinatum Tetramorium bicarinatum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8PWT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8PWT FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 15 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=8pwt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8pwt OCA], [https://pdbe.org/8pwt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8pwt RCSB], [https://www.ebi.ac.uk/pdbsum/8pwt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8pwt ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Ants are among the most abundant terrestrial invertebrate predators on Earth. To overwhelm their prey, they employ several remarkable behavioral, physiological, and biochemical innovations, including an effective paralytic venom. Ant venoms are thus cocktails of toxins finely tuned to disrupt the physiological systems of insect prey. They have received little attention yet hold great promise for the discovery of novel insecticidal molecules. To identify insect-neurotoxins from ant venoms, we screened the paralytic activity on blowflies of nine synthetic peptides previously characterized in the venom of Tetramorium bicarinatum. We selected peptide U(11), a 34-amino acid peptide, for further insecticidal, structural, and pharmacological experiments. Insecticidal assays revealed that U(11) is one of the most paralytic peptides ever reported from ant venoms against blowflies and is also capable of paralyzing honeybees. An NMR spectroscopy of U(11) uncovered a unique scaffold, featuring a compact triangular ring helix structure stabilized by a single disulfide bond. Pharmacological assays using Drosophila S2 cells demonstrated that U(11) is not cytotoxic, but suggest that it may modulate potassium conductance, which structural data seem to corroborate and will be confirmed in a future extended pharmacological investigation. The results described in this paper demonstrate that ant venom is a promising reservoir for the discovery of neuroactive insecticidal peptides.

Discovery of an Insect Neuroactive Helix Ring Peptide from Ant Venom.,Barasse V, Jouvensal L, Boy G, Billet A, Ascoet S, Lefranc B, Leprince J, Dejean A, Lacotte V, Rahioui I, Sivignon C, Gaget K, Ribeiro Lopes M, Calevro F, Da Silva P, Loth K, Paquet F, Treilhou M, Bonnafe E, Touchard A Toxins (Basel). 2023 Oct 5;15(10):600. doi: 10.3390/toxins15100600. PMID:37888631<ref>PMID:37888631</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Tetramorium bicarinatum]]
[[Category: Jouvensal L]]
[[Category: Loth K]]
[[Category: Paquet F]]