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<StructureSection load='7pxf' size='340' side='right'caption='[[7pxf]], [[Resolution|resolution]] 2.68&Aring;' scene=''>
<StructureSection load='7pxf' size='340' side='right'caption='[[7pxf]], [[Resolution|resolution]] 2.68&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7pxf]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PXF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PXF FirstGlance]. <br>
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PXF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PXF FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.68&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=7pxf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pxf OCA], [https://pdbe.org/7pxf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pxf RCSB], [https://www.ebi.ac.uk/pdbsum/7pxf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pxf 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=7pxf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pxf OCA], [https://pdbe.org/7pxf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pxf RCSB], [https://www.ebi.ac.uk/pdbsum/7pxf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pxf ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[[https://www.uniprot.org/uniprot/SLO_DROME SLO_DROME]] Potassium channel activated by both membrane depolarization or increase in cytosolic Ca(2+) that mediates export of K(+). Its activation dampens the excitatory events that elevate the cytosolic Ca(2+) concentration and/or depolarize the cell membrane. It therefore contributes to repolarization of the membrane potential. Kinetics are determined by alternative splicing, phosphorylation status and its combination interaction with Slob and 14-3-3-zeta. While the interaction with Slob1 alone increases its activity, its interaction with both Slob1 and 14-3-3-zeta decreases its activity.<ref>PMID:1497890</ref> <ref>PMID:1857984</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Slowpoke (Slo) potassium channels display extraordinarily high conductance, are synergistically activated by a positive transmembrane potential and high intracellular Ca(2+) concentrations and are important targets for insecticides and antiparasitic drugs. However, it is unknown how these compounds modulate ion translocation and whether there are insect-specific binding pockets. Here, we report structures of Drosophila Slo in the Ca(2+)-bound and Ca(2+)-free form and in complex with the fungal neurotoxin verruculogen and the anthelmintic drug emodepside. Whereas the architecture and gating mechanism of Slo channels are conserved, potential insect-specific binding pockets exist. Verruculogen inhibits K(+) transport by blocking the Ca(2+)-induced activation signal and precludes K(+) from entering the selectivity filter. Emodepside decreases the conductance by suboptimal K(+) coordination and uncouples ion gating from Ca(2+) and voltage sensing. Our results expand the mechanistic understanding of Slo regulation and lay the foundation for the rational design of regulators of Slo and other voltage-gated ion channels.


Small molecule modulation of the Drosophila Slo channel elucidated by cryo-EM.,Raisch T, Brockmann A, Ebbinghaus-Kintscher U, Freigang J, Gutbrod O, Kubicek J, Maertens B, Hofnagel O, Raunser S Nat Commun. 2021 Dec 9;12(1):7164. doi: 10.1038/s41467-021-27435-w. PMID:34887422<ref>PMID:34887422</ref>
==See Also==
 
*[[Potassium channel 3D structures|Potassium channel 3D structures]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7pxf" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Brockmann, A]]
[[Category: Brockmann A]]
[[Category: Ebbinghaus-Kintscher, U]]
[[Category: Ebbinghaus-Kintscher U]]
[[Category: Freigang, J]]
[[Category: Freigang J]]
[[Category: Gutbrod, O]]
[[Category: Gutbrod O]]
[[Category: Hofnagel, O]]
[[Category: Hofnagel O]]
[[Category: Kubicek, J]]
[[Category: Kubicek J]]
[[Category: Maertens, B]]
[[Category: Maertens B]]
[[Category: Raisch, T]]
[[Category: Raisch T]]
[[Category: Raunser, S]]
[[Category: Raunser S]]
[[Category: Bk channel]]
[[Category: Potassium transport]]
[[Category: Transport protein]]

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