2n1n
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Solution structure of VSTx1== | |
| + | <StructureSection load='2n1n' size='340' side='right'caption='[[2n1n]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2n1n]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Grammostola_rosea Grammostola rosea]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N1N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N1N 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=2n1n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n1n OCA], [https://pdbe.org/2n1n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n1n RCSB], [https://www.ebi.ac.uk/pdbsum/2n1n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n1n ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/VSTX1_GRARO VSTX1_GRARO] Inhibits sodium channels Nav1.7/SCN9A and potassium channels Kv11.1/KCNH2. Also binds the voltage-sensor domain of the potassium channel KvAP (from the archaeon Aeropyrum pernix) with very slow apparent binding kinetics and affects channel gating. Reaches its target by dynamically partitioning into anionic or zwitterionic headgroup lipid membranes. May bind to the open state of KvAP.<ref>PMID:15241419</ref> <ref>PMID:15287735</ref> <ref>PMID:17002285</ref> <ref>PMID:19955179</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Voltage-sensor domains (VSDs) are modular transmembrane domains of voltage-gated ion channels that respond to changes in membrane potential by undergoing conformational changes that are coupled to gating of the ion-conducting pore. Most spider-venom peptides function as gating modifiers by binding to the VSDs of voltage-gated channels and trapping them in a closed or open state. To understand the molecular basis underlying this mode of action, we used nuclear magnetic resonance to delineate the atomic details of the interaction between the VSD of the voltage-gated potassium channel KvAP and the spider-venom peptide VSTx1. Our data reveal that the toxin interacts with residues in an aqueous cleft formed between the extracellular S1-S2 and S3-S4 loops of the VSD whilst maintaining lipid interactions in the gaps formed between the S1-S4 and S2-S3 helices. The resulting network of interactions increases the energetic barrier to the conformational changes required for channel gating, and we propose that this is the mechanism by which gating modifier toxins inhibit voltage-gated ion channels. | ||
| - | + | Molecular basis of the interaction between gating modifier spider toxins and the voltage sensor of voltage-gated ion channels.,Lau CH, King GF, Mobli M Sci Rep. 2016 Sep 28;6:34333. doi: 10.1038/srep34333. PMID:27677715<ref>PMID:27677715</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 2n1n" style="background-color:#fffaf0;"></div> |
| - | [[Category: King | + | == References == |
| - | [[Category: Lau | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Grammostola rosea]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: King GF]] | ||
| + | [[Category: Lau HY]] | ||
| + | [[Category: Mobli M]] | ||
Current revision
Solution structure of VSTx1
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