2qks
From Proteopedia
(Difference between revisions)
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<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=2qks FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qks OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2qks RCSB], [http://www.ebi.ac.uk/pdbsum/2qks PDBsum]</span></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=2qks FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qks OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2qks RCSB], [http://www.ebi.ac.uk/pdbsum/2qks PDBsum]</span></td></tr> | ||
</table> | </table> | ||
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/IRK3_MOUSE IRK3_MOUSE]] This potassium channel is controlled by G proteins. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. This receptor plays a crucial role in regulating the heartbeat. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Burkholderia xenovorans]] | [[Category: Burkholderia xenovorans]] | ||
- | [[Category: MacKinnon, R | + | [[Category: MacKinnon, R]] |
- | [[Category: Nishida, M | + | [[Category: Nishida, M]] |
[[Category: Chimera]] | [[Category: Chimera]] | ||
[[Category: G-protein gated inward rectifier]] | [[Category: G-protein gated inward rectifier]] |
Revision as of 02:13, 25 December 2014
Crystal structure of a Kir3.1-prokaryotic Kir channel chimera
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