View source for 6ebl


==The voltage-activated Kv1.2-2.1 paddle chimera channel in lipid nanodiscs, cytosolic domain==
<SX load='6ebl' size='340' side='right' viewer='molstar' caption='[[6ebl]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6ebl]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EBL OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6EBL FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6ebl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ebl OCA], [http://pdbe.org/6ebl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ebl RCSB], [http://www.ebi.ac.uk/pdbsum/6ebl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ebl ProSAT]</span></td></tr>
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== Function ==
[[http://www.uniprot.org/uniprot/KCAB2_RAT KCAB2_RAT]] Accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. [[http://www.uniprot.org/uniprot/KCNA2_RAT KCNA2_RAT]] Mediates the voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient.<ref>PMID:7544443</ref>  
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== Publication Abstract from PubMed ==
Voltage-activated potassium (Kv) channels open to conduct K(+) ions in response to membrane depolarization, and subsequently enter non-conducting states through distinct mechanisms of inactivation. X-ray structures of detergent-solubilized Kv channels appear to have captured an open state even though a non-conducting C-type inactivated state would predominate in membranes in the absence of a transmembrane voltage. However, structures for a voltage-activated ion channel in a lipid bilayer environment have not yet been reported. Here we report the structure of the Kv1.2-2.1 paddle chimera channel reconstituted into lipid nanodiscs using single-particle cryo-electron microscopy. At a resolution of ~3 A for the cytosolic domain and ~4 A for the transmembrane domain, the structure determined in nanodiscs is similar to the previously determined X-ray structure. Our findings show that large differences in structure between detergent and lipid bilayer environments are unlikely, and enable us to propose possible structural mechanisms for C-type inactivation.

Single-particle cryo-EM structure of a voltage-activated potassium channel in lipid nanodiscs.,Matthies D, Bae C, Toombes GE, Fox T, Bartesaghi A, Subramaniam S, Swartz KJ Elife. 2018 Aug 15;7. pii: 37558. doi: 10.7554/eLife.37558. PMID:30109985<ref>PMID:30109985</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 6ebl" style="background-color:#fffaf0;"></div>

==See Also==
*[[Potassium channel 3D structures|Potassium channel 3D structures]]
== References ==
<references/>
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[[Category: Large Structures]]
[[Category: Bae, C]]
[[Category: Bartesaghi, A]]
[[Category: Fox, T]]
[[Category: Matthies, D]]
[[Category: Subramaniam, S]]
[[Category: Swartz, K J]]
[[Category: Lipid nanodisc]]
[[Category: Membrane protein]]
[[Category: Potassium channel]]
[[Category: Transport protein]]