View source for 6q61


==Pore-modulating toxins exploit inherent slow inactivation to block K+ channels==
<StructureSection load='6q61' size='340' side='right'caption='[[6q61]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6q61]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Conus_striatus Conus striatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Q61 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6Q61 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=6q61 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6q61 OCA], [https://pdbe.org/6q61 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6q61 RCSB], [https://www.ebi.ac.uk/pdbsum/6q61 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6q61 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/VKTS1_CONST VKTS1_CONST] Blocks specifically voltage-activated potassium channels (Kv) of the Shaker family (IC(50)=1.33 nM).<ref>PMID:15833744</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Voltage-dependent potassium channels (K(v)s) gate in response to changes in electrical membrane potential by coupling a voltage-sensing module with a K(+)-selective pore. Animal toxins targeting K(v)s are classified as pore blockers, which physically plug the ion conduction pathway, or as gating modifiers, which disrupt voltage sensor movements. A third group of toxins blocks K(+) conduction by an unknown mechanism via binding to the channel turrets. Here, we show that Conkunitzin-S1 (Cs1), a peptide toxin isolated from cone snail venom, binds at the turrets of K(v)1.2 and targets a network of hydrogen bonds that govern water access to the peripheral cavities that surround the central pore. The resulting ectopic water flow triggers an asymmetric collapse of the pore by a process resembling that of inherent slow inactivation. Pore modulation by animal toxins exposes the peripheral cavity of K(+) channels as a novel pharmacological target and provides a rational framework for drug design.

Pore-modulating toxins exploit inherent slow inactivation to block K(+) channels.,Karbat I, Altman-Gueta H, Fine S, Szanto T, Hamer-Rogotner S, Dym O, Frolow F, Gordon D, Panyi G, Gurevitz M, Reuveny E Proc Natl Acad Sci U S A. 2019 Sep 10;116(37):18700-18709. doi: , 10.1073/pnas.1908903116. Epub 2019 Aug 23. PMID:31444298<ref>PMID:31444298</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6q61" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Conus striatus]]
[[Category: Large Structures]]
[[Category: Dym O]]
[[Category: Fine S]]
[[Category: Frolow F]]
[[Category: Gordon D]]
[[Category: Gueta H]]
[[Category: Gurevitz M]]
[[Category: Hamer-Rogotner S]]
[[Category: Karbat I]]
[[Category: Panyi G]]
[[Category: Reuveny E]]
[[Category: Szanto T]]