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1n9p

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(New page: 200px<br /><applet load="1n9p" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n9p, resolution 1.80&Aring;" /> '''Crystal Structure of...)
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[[Image:1n9p.jpg|left|200px]]<br /><applet load="1n9p" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1n9p, resolution 1.80&Aring;" />
 
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'''Crystal Structure of the Cytoplasmic Domain of G-protein Activated Inward Rectifier Potassium Channel 1'''<br />
 
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==Overview==
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==Crystal Structure of the Cytoplasmic Domain of G-protein Activated Inward Rectifier Potassium Channel 1==
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Inward rectifier K(+) channels govern the resting membrane voltage in many, cells. Regulation of these ion channels via G protein-coupled receptor, signaling underlies the control of heart rate and the actions of, neurotransmitters in the central nervous system. We have determined the, protein structure formed by the intracellular N- and C termini of the G, protein-gated inward rectifier K(+) channel GIRK1 at 1.8 A resolution. A, cytoplasmic pore, conserved among inward rectifier K(+) channels, extends, the ion pathway to 60 A, nearly twice the length of a canonical, transmembrane K(+) channel. The cytoplasmic pore is lined by acidic and, hydrophobic amino acids, creating a favorable environment for polyamines, which block the pore. These results explain in structural and chemical, terms the basis of inward rectification, and they also have implications, for G protein regulation of GIRK channels.
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<StructureSection load='1n9p' size='340' side='right'caption='[[1n9p]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1n9p]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N9P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N9P FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1n9p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n9p OCA], [https://pdbe.org/1n9p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n9p RCSB], [https://www.ebi.ac.uk/pdbsum/1n9p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n9p ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/KCNJ3_MOUSE KCNJ3_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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/n9/1n9p_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1n9p ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1N9P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1N9P OCA].
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*[[Potassium channel 3D structures|Potassium channel 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Structural basis of inward rectification: cytoplasmic pore of the G protein-gated inward rectifier GIRK1 at 1.8 A resolution., Nishida M, MacKinnon R, Cell. 2002 Dec 27;111(7):957-65. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12507423 12507423]
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[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Single protein]]
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[[Category: MacKinnon R]]
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[[Category: MacKinnon, R.]]
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[[Category: Nishida M]]
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[[Category: Nishida, M.]]
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[[Category: beta barrel]]
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[[Category: cytoplasmic domain]]
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[[Category: g protein]]
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[[Category: inward rectifier]]
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[[Category: potassium channel]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:04:59 2007''
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Current revision

Crystal Structure of the Cytoplasmic Domain of G-protein Activated Inward Rectifier Potassium Channel 1

PDB ID 1n9p

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