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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== 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/initialview03.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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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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==About this Structure==
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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:12507423<ref>PMID:12507423</ref>
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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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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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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</div>
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[[Category: Mus musculus]]
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<div class="pdbe-citations 1n9p" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: MacKinnon, R.]]
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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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==See Also==
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*[[Potassium channel 3D structures|Potassium channel 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Mus musculus]]
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[[Category: MacKinnon R]]
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[[Category: Nishida M]]

Current revision

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

PDB ID 1n9p

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