7s5v
From Proteopedia
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==Human KATP channel in open conformation, focused on SUR== | ==Human KATP channel in open conformation, focused on SUR== | ||
| - | <StructureSection load='7s5v' size='340' side='right'caption='[[7s5v]]' scene=''> | + | <StructureSection load='7s5v' size='340' side='right'caption='[[7s5v]], [[Resolution|resolution]] 3.30Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7S5V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7S5V FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7s5v]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7S5V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7S5V FirstGlance]. <br> |
| - | </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=7s5v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7s5v OCA], [https://pdbe.org/7s5v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7s5v RCSB], [https://www.ebi.ac.uk/pdbsum/7s5v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7s5v ProSAT]</span></td></tr> | + | </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=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[7s5t|7s5t]]</div></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=7s5v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7s5v OCA], [https://pdbe.org/7s5v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7s5v RCSB], [https://www.ebi.ac.uk/pdbsum/7s5v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7s5v ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Disease == | ||
| + | [[https://www.uniprot.org/uniprot/ABCC8_HUMAN ABCC8_HUMAN]] Diazoxide-resistant focal hyperinsulinism due to SUR1 deficiency;Autosomal dominant hyperinsulinism due to SUR1 deficiency;Transient neonatal diabetes mellitus;DEND syndrome;Autosomal recessive hyperinsulinism due to SUR1 deficiency;MODY;Permanent neonatal diabetes mellitus. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/ABCC8_HUMAN ABCC8_HUMAN]] Subunit of the beta-cell ATP-sensitive potassium channel (KATP). Regulator of ATP-sensitive K(+) channels and insulin release.<ref>PMID:24814349</ref> <ref>PMID:25720052</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | KATP channels are metabolic sensors that translate intracellular ATP/ADP balance into membrane excitability. The molecular composition of KATP includes an inward-rectifier potassium channel (Kir) and an ABC transporter-like sulfonylurea receptor (SUR). Although structures of KATP have been determined in many conformations, in all cases, the pore in Kir is closed. Here, we describe human pancreatic KATP (hKATP) structures with an open pore at 3.1- to 4.0-A resolution using single-particle cryo-electron microscopy (cryo-EM). Pore opening is associated with coordinated structural changes within the ATP-binding site and the channel gate in Kir. Conformational changes in SUR are also observed, resulting in an area reduction of contact surfaces between SUR and Kir. We also observe that pancreatic hKATP exhibits the unique (among inward-rectifier channels) property of PIP2-independent opening, which appears to be correlated with a docked cytoplasmic domain in the absence of PIP2. | ||
| + | |||
| + | Molecular structure of an open human KATP channel.,Zhao C, MacKinnon R Proc Natl Acad Sci U S A. 2021 Nov 30;118(48). pii: 2112267118. doi:, 10.1073/pnas.2112267118. PMID:34815345<ref>PMID:34815345</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7s5v" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: MacKinnon R]] | + | [[Category: MacKinnon, R]] |
| - | [[Category: Zhao C]] | + | [[Category: Zhao, C]] |
| + | [[Category: Atp-sensitive potassium channel]] | ||
| + | [[Category: Ion channel]] | ||
| + | [[Category: Katp]] | ||
| + | [[Category: Membrane protein]] | ||
Revision as of 10:10, 8 December 2021
Human KATP channel in open conformation, focused on SUR
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