5mou
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==NMR spatial structure of scorpion alpha-like toxin BeM9== | |
| + | <StructureSection load='5mou' size='340' side='right'caption='[[5mou]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5mou]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mesobuthus_eupeus Mesobuthus eupeus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MOU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MOU FirstGlance]. <br> | ||
| + | </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=5mou FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mou OCA], [https://pdbe.org/5mou PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mou RCSB], [https://www.ebi.ac.uk/pdbsum/5mou PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mou ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/SCX9_MESEU SCX9_MESEU] Alpha toxins bind voltage-independently at site-3 of sodium channels (Nav) and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission. Has paralytic activity in mice. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Sodium channel alpha-toxins from scorpion venom (alpha-NaTx) inhibit the inactivation of voltage-gated sodium channels. We used solution NMR to investigate the structure of BeM9 toxin from Mesobuthus eupeus scorpion, a prototype alpha-NaTx classified as an "alpha-like" toxin due to its wide spectrum of activity on insect and mammalian channels. We identified a new motif that we named "arginine hand", whereby arginine side chain forms several hydrogen bonds with main chain atoms. The arginine hand was found in the "specificity module", a part of the molecule that dictates toxin selectivity; and just single arginine-to-lysine point mutation drastically changed BeM9 selectivity profile. This article is protected by copyright. All rights reserved. | ||
| - | + | Refined structure of BeM9 reveals arginine hand, an overlooked structural motif in scorpion toxins affecting sodium channels.,Kuldyushev NA, Mineev KS, Berkut AA, Peigneur S, Arseniev AS, Tytgat J, Grishin EV, Vassilevski AA Proteins. 2018 Jul 14. doi: 10.1002/prot.25583. PMID:30007037<ref>PMID:30007037</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 5mou" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: Berkut | + | <references/> |
| - | [[Category: | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| - | [[Category: | + | [[Category: Large Structures]] |
| + | [[Category: Mesobuthus eupeus]] | ||
| + | [[Category: Arseniev AS]] | ||
| + | [[Category: Berkut AA]] | ||
| + | [[Category: Grishin EV]] | ||
| + | [[Category: Kuldushev NA]] | ||
| + | [[Category: Mineev KS]] | ||
| + | [[Category: Vassilevski AA]] | ||
Current revision
NMR spatial structure of scorpion alpha-like toxin BeM9
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