7pxg

<table><tr><td colspan='2'>[[7pxg]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PXG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PXG FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6PL:(4S,7R)-4-HYDROXY-N,N,N-TRIMETHYL-9-OXO-7-[(PALMITOYLOXY)METHYL]-3,5,8-TRIOXA-4-PHOSPHAHEXACOSAN-1-AMINIUM+4-OXIDE'>6PL</scene>, <scene name='pdbligand=8H5:Verruculogen'>8H5</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CLR:CHOLESTEROL'>CLR</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>

== 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>

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== 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.

 

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== References ==

[[Category: Brockmann, A]]

[[Category: Ebbinghaus-Kintscher, U]]

[[Category: Freigang, J]]

[[Category: Gutbrod, O]]

[[Category: Hofnagel, O]]

[[Category: Kubicek, J]]

[[Category: Maertens, B]]

[[Category: Raisch, T]]

[[Category: Raunser, S]]

[[Category: Transport protein]]