1qrq

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<StructureSection load='1qrq' size='340' side='right'caption='[[1qrq]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
<StructureSection load='1qrq' size='340' side='right'caption='[[1qrq]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1qrq]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QRQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QRQ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1qrq]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QRQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QRQ FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene></td></tr>
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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]] 2.8&#8491;</td></tr>
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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=1qrq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qrq OCA], [http://pdbe.org/1qrq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qrq RCSB], [http://www.ebi.ac.uk/pdbsum/1qrq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1qrq ProSAT]</span></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=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</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=1qrq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qrq OCA], [https://pdbe.org/1qrq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qrq RCSB], [https://www.ebi.ac.uk/pdbsum/1qrq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qrq ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/KCAB2_RAT KCAB2_RAT]] Accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
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[https://www.uniprot.org/uniprot/KCAB2_RAT KCAB2_RAT] Accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1qrq ConSurf].
</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=1qrq ConSurf].
<div style="clear:both"></div>
<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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The integral membrane subunits of many voltage-dependent potassium channels are associated with an additional protein known as the beta subunit. One function of beta subunits is to modify K+ channel gating. We have determined the structure of the conserved core of mammalian beta subunits by X-ray crystallography at 2.8 A resolution. Like the integral membrane component of K+ channels, beta subunits form a four-fold symmetric structure. Each subunit is an oxidoreductase enzyme complete with a nicotinamide co-factor in its active site. Several structural features of the enzyme active site, including its location with respect to the four-fold axis, imply that it may interact directly or indirectly with the K+ channel's voltage sensor. This structure suggests a mechanism for coupling membrane electrical excitability directly to chemistry of the cell.
 
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Structure of a voltage-dependent K+ channel beta subunit.,Gulbis JM, Mann S, MacKinnon R Cell. 1999 Jun 25;97(7):943-52. PMID:10399921<ref>PMID:10399921</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 1qrq" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
*[[Ion channels|Ion channels]]
*[[Ion channels|Ion channels]]
*[[Potassium channel 3D structures|Potassium channel 3D structures]]
*[[Potassium channel 3D structures|Potassium channel 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Buffalo rat]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Gulbis, J M]]
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[[Category: Rattus norvegicus]]
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[[Category: MacKinnon, R]]
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[[Category: Gulbis JM]]
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[[Category: Mann, S]]
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[[Category: MacKinnon R]]
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[[Category: Aldo-keto reductase]]
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[[Category: Mann S]]
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[[Category: Metal transport]]
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[[Category: Potassium channel subunit]]
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[[Category: Tim barrel]]
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[[Category: Voltage-dependent potassium channel]]
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Current revision

STRUCTURE OF A VOLTAGE-DEPENDENT K+ CHANNEL BETA SUBUNIT

PDB ID 1qrq

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