6ebk: Difference between revisions

<StructureSection load='6ebk' size='340' side='right' caption='[[6ebk]], [[Resolution|resolution]] 3.30&Aring;' scene=''>

<table><tr><td colspan='2'>[[6ebk]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EBK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6EBK FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ebk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ebk OCA], [http://pdbe.org/6ebk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ebk RCSB], [http://www.ebi.ac.uk/pdbsum/6ebk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ebk ProSAT]</span></td></tr>

[[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> 

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.

 

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== References ==

</StructureSection>

[[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: Transport protein]]