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''' | ==Cryo-EM structure of the Slo2.2 Na-activated K channel== | ||
<StructureSection load='5a6e' size='340' side='right' caption='[[5a6e]], [[Resolution|resolution]] 4.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5a6e]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A6E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5A6E FirstGlance]. <br> | |||
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5a6f|5a6f]], [[5a6g|5a6g]]</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=5a6e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a6e OCA], [http://pdbe.org/5a6e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5a6e RCSB], [http://www.ebi.ac.uk/pdbsum/5a6e PDBsum]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/KCNT1_CHICK KCNT1_CHICK]] Generates outwardly rectifying currents that are suppressed by elevation of intracellular calcium. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Na+-activated K+ channels are members of the Slo family of large conductance K+ channels that are widely expressed in the brain, where their opening regulates neuronal excitability. These channels fulfil a number of biological roles and have intriguing biophysical properties, including conductance levels that are ten times those of most other K+ channels and gating sensitivity to intracellular Na+. Here we present the structure of a complete Na+-activated K+ channel, chicken Slo2.2, in the Na+-free state, determined by cryo-electron microscopy at a nominal resolution of 4.5 angstroms. The channel is composed of a large cytoplasmic gating ring, in which resides the Na+-binding site and a transmembrane domain that closely resembles voltage-gated K+ channels. In the structure, the cytoplasmic domain adopts a closed conformation and the ion conduction pore is also closed. The structure reveals features that can explain the unusually high conductance of Slo channels and how contraction of the cytoplasmic gating ring closes the pore. | |||
Cryo-electron microscopy structure of the Slo2.2 Na-activated K channel.,Hite RK, Yuan P, Li Z, Hsuing Y, Walz T, MacKinnon R Nature. 2015 Oct 5. doi: 10.1038/nature14958. PMID:26436452<ref>PMID:26436452</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5a6e" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
[[Category: | __TOC__ | ||
</StructureSection> | |||
[[Category: Hite, R K]] | |||
[[Category: Hsuing, Y]] | [[Category: Hsuing, Y]] | ||
[[Category: | [[Category: Li, Z]] | ||
[[Category: MacKinnon, R]] | |||
[[Category: Walz, T]] | [[Category: Walz, T]] | ||
[[Category: | [[Category: Yuan, P]] | ||
[[Category: Ion channel]] | |||
[[Category: Potassium channel]] | |||
[[Category: Transport]] | |||
Revision as of 06:49, 16 October 2015
Cryo-EM structure of the Slo2.2 Na-activated K channelCryo-EM structure of the Slo2.2 Na-activated K channel
Structural highlights
Function[KCNT1_CHICK] Generates outwardly rectifying currents that are suppressed by elevation of intracellular calcium. Publication Abstract from PubMedNa+-activated K+ channels are members of the Slo family of large conductance K+ channels that are widely expressed in the brain, where their opening regulates neuronal excitability. These channels fulfil a number of biological roles and have intriguing biophysical properties, including conductance levels that are ten times those of most other K+ channels and gating sensitivity to intracellular Na+. Here we present the structure of a complete Na+-activated K+ channel, chicken Slo2.2, in the Na+-free state, determined by cryo-electron microscopy at a nominal resolution of 4.5 angstroms. The channel is composed of a large cytoplasmic gating ring, in which resides the Na+-binding site and a transmembrane domain that closely resembles voltage-gated K+ channels. In the structure, the cytoplasmic domain adopts a closed conformation and the ion conduction pore is also closed. The structure reveals features that can explain the unusually high conductance of Slo channels and how contraction of the cytoplasmic gating ring closes the pore. Cryo-electron microscopy structure of the Slo2.2 Na-activated K channel.,Hite RK, Yuan P, Li Z, Hsuing Y, Walz T, MacKinnon R Nature. 2015 Oct 5. doi: 10.1038/nature14958. PMID:26436452[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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