6v3c: Difference between revisions

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-'''Unreleased structure'''
-The entry 6v3c is ON HOLD  until Paper Publication
+==K2P2.1(TREK-1)I110D:Ru360 bound channel structure==
+<StructureSection load='6v3c' size='340' side='right'caption='[[6v3c]], [[Resolution|resolution]] 3.51&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6v3c]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6V3C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6V3C FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=HEX:HEXANE'>HEX</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=LNK:PENTANE'>LNK</scene>, <scene name='pdbligand=OCT:N-OCTANE'>OCT</scene>, <scene name='pdbligand=RU3:ruthenium(6+)+formate+azanide+tetraamino(formato-kappaO)oxidoruthenate(1-)+(1/1/4/1)'>RU3</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6v3c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6v3c OCA], [http://pdbe.org/6v3c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6v3c RCSB], [http://www.ebi.ac.uk/pdbsum/6v3c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6v3c ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The trinuclear ruthenium amine ruthenium red (RuR) inhibits diverse ion channels, including K2P potassium channels, TRPs, the calcium uniporter, CALHMs, ryanodine receptors, and Piezos. Despite this extraordinary array, there is limited information for how RuR engages targets. Here, using X-ray crystallographic and electrophysiological studies of an RuR-sensitive K2P, K2P2.1 (TREK-1) I110D, we show that RuR acts by binding an acidic residue pair comprising the "Keystone inhibitor site" under the K2P CAP domain archway above the channel pore. We further establish that Ru360, a dinuclear ruthenium amine not known to affect K2Ps, inhibits RuR-sensitive K2Ps using the same mechanism. Structural knowledge enabled a generalizable design strategy for creating K2P RuR "super-responders" having nanomolar sensitivity. Together, the data define a "finger in the dam" inhibition mechanism acting at a novel K2P inhibitor binding site. These findings highlight the polysite nature of K2P pharmacology and provide a new framework for K2P inhibitor development.
-Authors:
+Polynuclear Ruthenium Amines Inhibit K2P Channels via a "Finger in the Dam" Mechanism.,Pope L, Lolicato M, Minor DL Jr Cell Chem Biol. 2020 Feb 10. pii: S2451-9456(20)30036-2. doi:, 10.1016/j.chembiol.2020.01.011. PMID:32059793<ref>PMID:32059793</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6v3c" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Lolicato, M]]
+[[Category: Minor, D L]]
+[[Category: Pope, L]]
+[[Category: K channel]]
+[[Category: Membrane protein]]
+[[Category: Mus musculus]]
+[[Category: Trek-1]]