7vls: Difference between revisions

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<StructureSection load='7vls' size='340' side='right'caption='[[7vls]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
<StructureSection load='7vls' size='340' side='right'caption='[[7vls]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7vls]] is a 1 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=7VLS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7VLS FirstGlance]. <br>
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7VLS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7VLS FirstGlance]. <br>
</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=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=ESV:1-cyano-2-(2-methylbutan-2-yl)-3-pyridin-3-yl-guanidine'>ESV</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=Y01:CHOLESTEROL+HEMISUCCINATE'>Y01</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.3&#8491;</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=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=ESV:1-cyano-2-(2-methylbutan-2-yl)-3-pyridin-3-yl-guanidine'>ESV</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=Y01:CHOLESTEROL+HEMISUCCINATE'>Y01</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7vls FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7vls OCA], [https://pdbe.org/7vls PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7vls RCSB], [https://www.ebi.ac.uk/pdbsum/7vls PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7vls ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7vls FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7vls OCA], [https://pdbe.org/7vls PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7vls RCSB], [https://www.ebi.ac.uk/pdbsum/7vls PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7vls ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ABCC9_RAT ABCC9_RAT] Subunit of ATP-sensitive potassium channels (KATP). Can form cardiac and smooth muscle-type KATP channels with KCNJ11. KCNJ11 forms the channel pore while ABCC9 is required for activation and regulation.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
ATP-sensitive potassium channels (K(ATP)), composed of Kir6 and SUR subunits, convert the metabolic status of the cell into electrical signals. Pharmacological activation of SUR2- containing K(ATP) channels by class of small molecule drugs known as K(ATP) openers leads to hyperpolarization of excitable cells and to vasodilation. Thus, K(ATP) openers could be used to treat cardiovascular diseases. However, where these vasodilators bind to K(ATP) and how they activate the channel remains elusive. Here, we present cryo-EM structures of SUR2A and SUR2B subunits in complex with Mg-nucleotides and P1075 or levcromakalim, two chemically distinct K(ATP) openers that are specific to SUR2. Both P1075 and levcromakalim bind to a common site in the transmembrane domain (TMD) of the SUR2 subunit, which is between TMD1 and TMD2 and is embraced by TM10, TM11, TM12, TM14, and TM17. These K(ATP) openers synergize with Mg-nucleotides to stabilize SUR2 in the NBD-dimerized occluded state to activate the channel.
Structural identification of vasodilator binding sites on the SUR2 subunit.,Ding D, Wu JX, Duan X, Ma S, Lai L, Chen L Nat Commun. 2022 May 13;13(1):2675. doi: 10.1038/s41467-022-30428-y. PMID:35562524<ref>PMID:35562524</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7vls" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[ABC transporter 3D structures|ABC transporter 3D structures]]
*[[ABC transporter 3D structures|ABC transporter 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Chen L]]
[[Category: Chen L]]
[[Category: Ding D]]
[[Category: Ding D]]

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