8bo0
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[8bo0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Leiurus_quinquestriatus_quinquestriatus Leiurus quinquestriatus quinquestriatus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8BO0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8BO0 FirstGlance]. <br> | <table><tr><td colspan='2'>[[8bo0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Leiurus_quinquestriatus_quinquestriatus Leiurus quinquestriatus quinquestriatus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8BO0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8BO0 FirstGlance]. <br> | ||
| - | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | + | </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=8bo0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8bo0 OCA], [https://pdbe.org/8bo0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8bo0 RCSB], [https://www.ebi.ac.uk/pdbsum/8bo0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8bo0 ProSAT]</span></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=8bo0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8bo0 OCA], [https://pdbe.org/8bo0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8bo0 RCSB], [https://www.ebi.ac.uk/pdbsum/8bo0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8bo0 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | [https://www.uniprot.org/uniprot/SCX4_LEIQU SCX4_LEIQU] | + | [https://www.uniprot.org/uniprot/SCX4_LEIQU SCX4_LEIQU] Alpha toxins bind voltage-independently at site-3 of sodium channels (Nav) and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission. Both native and recombinant (non-amidated) toxins inhibit inactivation of Nav1.2/SCN2A (EC(50)=31.2-36.6 nM), Nav1.6/SCN8A (EC(50)=6.9-8.9 nM), and Nav1.7/SCN9A (EC(50)=182.0-260.1 nM).<ref>PMID:37501371</ref> |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Scorpion alpha-toxins (alpha-NaTx) inhibiting the inactivation of voltage-gated sodium channels (Na(v) ) are a well-studied family of small proteins. We previously showed that the structure of alpha-NaTx specificity module responsible for selective Na(v) binding is governed by an interplay between the nest and niche protein motifs. Here, we report the solution structure of the toxin Lqq4 from the venom of the scorpion Leiurus quinquestriatus. Unexpectedly, we find that this toxin presents an ensemble of long-lived structurally distinct states. We unequivocally assign these states to the alternative configurations (cis-trans isomers) of two peptide bonds: V56-P57 and C17-G18; neither of the cis isomers has been described in alpha-NaTx so far. We argue that the native conformational space of alpha-NaTx is wider than assumed previously. | Scorpion alpha-toxins (alpha-NaTx) inhibiting the inactivation of voltage-gated sodium channels (Na(v) ) are a well-studied family of small proteins. We previously showed that the structure of alpha-NaTx specificity module responsible for selective Na(v) binding is governed by an interplay between the nest and niche protein motifs. Here, we report the solution structure of the toxin Lqq4 from the venom of the scorpion Leiurus quinquestriatus. Unexpectedly, we find that this toxin presents an ensemble of long-lived structurally distinct states. We unequivocally assign these states to the alternative configurations (cis-trans isomers) of two peptide bonds: V56-P57 and C17-G18; neither of the cis isomers has been described in alpha-NaTx so far. We argue that the native conformational space of alpha-NaTx is wider than assumed previously. | ||
| - | A scorpion toxin affecting sodium channels shows double cis-trans isomerism.,Mineev KS, Chernykh MA, Motov VV, Prudnikova DA, Pavlenko DM, Kuzmenkov AI, Peigneur S, Tytgat J, Vassilevski AA FEBS Lett. 2023 | + | A scorpion toxin affecting sodium channels shows double cis-trans isomerism.,Mineev KS, Chernykh MA, Motov VV, Prudnikova DA, Pavlenko DM, Kuzmenkov AI, Peigneur S, Tytgat J, Vassilevski AA FEBS Lett. 2023 Sep;597(18):2358-2368. doi: 10.1002/1873-3468.14705. Epub 2023 , Aug 7. PMID:37501371<ref>PMID:37501371</ref> |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
Current revision
Solution structure of Lqq4 toxin from Leiurus quinquestriatus quinquestriatus
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