5ywd

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Current revision (10:25, 27 March 2024) (edit) (undo)
 
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<SX load='5ywd' size='340' side='right' viewer='molstar' caption='[[5ywd]], [[Resolution|resolution]] 4.20&Aring;' scene=''>
<SX load='5ywd' size='340' side='right' viewer='molstar' caption='[[5ywd]], [[Resolution|resolution]] 4.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5ywd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Golden_hamster Golden hamster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YWD OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5YWD FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5ywd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mesocricetus_auratus Mesocricetus auratus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YWD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YWD FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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">Electron Microscopy, [[Resolution|Resolution]] 4.2&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Abcc8 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10036 Golden hamster])</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=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5ywd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ywd OCA], [http://pdbe.org/5ywd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ywd RCSB], [http://www.ebi.ac.uk/pdbsum/5ywd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ywd ProSAT]</span></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=5ywd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ywd OCA], [https://pdbe.org/5ywd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ywd RCSB], [https://www.ebi.ac.uk/pdbsum/5ywd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ywd ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/A0A1U7R319_MESAU A0A1U7R319_MESAU]
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ATP-sensitive potassium channels (KATP) are energy sensors on the plasma membrane. By sensing the intracellular ADP/ATP ratio of beta-cells, pancreatic KATP channels control insulin release and regulate metabolism at the whole body level. They are implicated in many metabolic disorders and diseases and are therefore important drug targets. Here, we present three structures of pancreatic KATP channels solved by cryo-electron microscopy (cryo-EM), at resolutions ranging from 4.1 to 4.5 A. These structures depict the binding site of the antidiabetic drug glibenclamide, indicate how Kir6.2 (inward-rectifying potassium channel 6.2) N-terminus participates in the coupling between the peripheral SUR1 (sulfonylurea receptor 1) subunit and the central Kir6.2 channel, reveal the binding mode of activating nucleotides, and suggest the mechanism of how Mg-ADP binding on nucleotide binding domains (NBDs) drives a conformational change of the SUR1 subunit.
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Ligand binding and conformational changes of SUR1 subunit in pancreatic ATP-sensitive potassium channels.,Wu JX, Ding D, Wang M, Kang Y, Zeng X, Chen L Protein Cell. 2018 Mar 28. pii: 10.1007/s13238-018-0530-y. doi:, 10.1007/s13238-018-0530-y. PMID:29594720<ref>PMID:29594720</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 5ywd" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</SX>
</SX>
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[[Category: Golden hamster]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Chen, L]]
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[[Category: Mesocricetus auratus]]
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[[Category: Wu, J X]]
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[[Category: Chen L]]
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[[Category: Channel]]
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[[Category: Wu JX]]
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[[Category: Glibenclamide]]
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[[Category: Katp]]
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[[Category: Membrane protein]]
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[[Category: Sulfonylurea]]
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Current revision

Structure of pancreatic ATP-sensitive potassium channel bound with Mg-ADP (focused refinement of SUR1 ABC transporter module at 4.22A)

5ywd, resolution 4.20Å

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