3k6n

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{{Seed}}
 
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[[Image:3k6n.png|left|200px]]
 
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==Crystal structure of the S225E mutant Kir3.1 cytoplasmic pore domain==
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The line below this paragraph, containing "STRUCTURE_3k6n", creates the "Structure Box" on the page.
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<StructureSection load='3k6n' size='340' side='right'caption='[[3k6n]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3k6n]] 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=3K6N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3K6N FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2&#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=NA:SODIUM+ION'>NA</scene></td></tr>
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{{STRUCTURE_3k6n| PDB=3k6n | SCENE= }}
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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=3k6n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k6n OCA], [https://pdbe.org/3k6n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3k6n RCSB], [https://www.ebi.ac.uk/pdbsum/3k6n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3k6n 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/k6/3k6n_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=3k6n ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Strong voltage sensitivity of inward-rectifier K(+) (Kir) channels has been hypothesized to arise primarily from an intracellular blocker displacing up to five K(+) ions from the wide, intracellular part of the ion conduction pore outwardly across the narrow ion-selectivity filter. The validity of this hypothesis depends on two assumptions: (i) that five ion sites are located intracellular to the filter and (ii) that the blocker can force essentially unidirectional K(+) movement in a pore region generally wider than the combined dimensions of the blocker plus a K(+) ion. Here we present a crystal structure of the cytoplasmic portion of a Kir channel with five ions bound and demonstrate that a constriction near the intracellular end of the pore, acting as a gasket, prevents K(+) ions from bypassing the blocker. This heretofore unrecognized 'gasket' ensures that the blocker can effectively displace K(+) ions across the selectivity filter to generate exceedingly strong voltage sensitivity.
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===Crystal structure of the S225E mutant Kir3.1 cytoplasmic pore domain===
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Physical determinants of strong voltage sensitivity of K(+) channel block.,Xu Y, Shin HG, Szep S, Lu Z Nat Struct Mol Biol. 2009 Dec;16(12):1252-8. Epub 2009 Nov 15. PMID:19915587<ref>PMID:19915587</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3k6n" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_19915587}}, adds the Publication Abstract to the page
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*[[Potassium channel 3D structures|Potassium channel 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 19915587 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_19915587}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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3K6N is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3K6N OCA].
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==Reference==
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<ref group="xtra">PMID:19915587</ref><references group="xtra"/>
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Lu, Z.]]
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[[Category: Lu Z]]
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[[Category: Shin, H G.]]
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[[Category: Shin HG]]
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[[Category: Szep, S.]]
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[[Category: Szep S]]
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[[Category: Xu, Y.]]
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[[Category: Xu Y]]
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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: Ion transport]]
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[[Category: Ionic channel]]
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[[Category: Metal transport]]
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[[Category: Potassium channel]]
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[[Category: Transmembrane]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 16 11:55:56 2009''
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Current revision

Crystal structure of the S225E mutant Kir3.1 cytoplasmic pore domain

PDB ID 3k6n

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