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==Cryo-EM structure of the pancreatic ATP-sensitive K+ channel SUR1/Kir6.2 in the presence of ATP and glibenclamide== | |||
<StructureSection load='5twv' size='340' side='right' caption='[[5twv]], [[Resolution|resolution]] 6.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5twv]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TWV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TWV FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene></td></tr> | |||
<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=5twv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5twv OCA], [http://pdbe.org/5twv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5twv RCSB], [http://www.ebi.ac.uk/pdbsum/5twv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5twv ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/ABCC8_CRICR ABCC8_CRICR]] Subunit of the beta-cell ATP-sensitive potassium channel (KATP). Regulator of ATP-sensitive potassium channels and insulin release.[UniProtKB:Q09428] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
KATP channels are metabolic sensors that couple cell energetics to membrane excitability. In pancreatic beta-cells, channels formed by SUR1 and Kir6.2 regulate insulin secretion and are the targets of antidiabetic sulfonylureas. Here, we used cryo-EM to elucidate structural basis of channel assembly and gating. The structure, determined in the presence of ATP and the sulfonylurea glibenclamide, at ~6A resolution reveals a closed Kir6.2 tetrameric core with four peripheral SUR1s each anchored to a Kir6.2 by its N-terminal transmembrane domain (TMD0). Intricate interactions between TMD0, the loop following TMD0, and Kir6.2 near the proposed PIP2 binding site, and where ATP density is observed, suggest SUR1 may contribute to ATP and PIP2 binding to enhance Kir6.2 sensitivity to both. The SUR1-ABC core is found in an unusual inward-facing conformation whereby the two nucleotide binding domains are misaligned along a two-fold symmetry axis, revealing a possible mechanism by which glibenclamide inhibits channel activity. | |||
Cryo-EM structure of the ATP-sensitive potassium channel illuminates mechanisms of assembly and gating.,Martin GM, Yoshioka C, Rex EA, Fay JF, Xie Q, Whorton MR, Chen JZ, Shyng SL Elife. 2017 Jan 16;6. pii: e24149. doi: 10.7554/eLife.24149. PMID:28092267<ref>PMID:28092267</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5twv" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Chen, J Z]] | |||
[[Category: Martin, G M]] | |||
[[Category: Shyng, S L]] | |||
[[Category: Yoshioka, C]] | |||
[[Category: Abc transporter]] | |||
[[Category: Ion channel]] | |||
[[Category: Membrane protein]] | |||
[[Category: Potassium channel]] | |||
[[Category: Transport protein]] | |||
Revision as of 02:36, 26 January 2017
Cryo-EM structure of the pancreatic ATP-sensitive K+ channel SUR1/Kir6.2 in the presence of ATP and glibenclamideCryo-EM structure of the pancreatic ATP-sensitive K+ channel SUR1/Kir6.2 in the presence of ATP and glibenclamide
Structural highlights
Function[ABCC8_CRICR] Subunit of the beta-cell ATP-sensitive potassium channel (KATP). Regulator of ATP-sensitive potassium channels and insulin release.[UniProtKB:Q09428] Publication Abstract from PubMedKATP channels are metabolic sensors that couple cell energetics to membrane excitability. In pancreatic beta-cells, channels formed by SUR1 and Kir6.2 regulate insulin secretion and are the targets of antidiabetic sulfonylureas. Here, we used cryo-EM to elucidate structural basis of channel assembly and gating. The structure, determined in the presence of ATP and the sulfonylurea glibenclamide, at ~6A resolution reveals a closed Kir6.2 tetrameric core with four peripheral SUR1s each anchored to a Kir6.2 by its N-terminal transmembrane domain (TMD0). Intricate interactions between TMD0, the loop following TMD0, and Kir6.2 near the proposed PIP2 binding site, and where ATP density is observed, suggest SUR1 may contribute to ATP and PIP2 binding to enhance Kir6.2 sensitivity to both. The SUR1-ABC core is found in an unusual inward-facing conformation whereby the two nucleotide binding domains are misaligned along a two-fold symmetry axis, revealing a possible mechanism by which glibenclamide inhibits channel activity. Cryo-EM structure of the ATP-sensitive potassium channel illuminates mechanisms of assembly and gating.,Martin GM, Yoshioka C, Rex EA, Fay JF, Xie Q, Whorton MR, Chen JZ, Shyng SL Elife. 2017 Jan 16;6. pii: e24149. doi: 10.7554/eLife.24149. PMID:28092267[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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