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| | <SX load='5twv' size='340' side='right' viewer='molstar' caption='[[5twv]], [[Resolution|resolution]] 6.30Å' scene=''> | | <SX load='5twv' size='340' side='right' viewer='molstar' caption='[[5twv]], [[Resolution|resolution]] 6.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5twv]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Black-bellied_hamster Black-bellied hamster] and [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. 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> | + | <table><tr><td colspan='2'>[[5twv]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Cricetus_cricetus Cricetus cricetus] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. 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 [https://proteopedia.org/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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 6.3Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Kcnj11 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat]), ABCC8, SUR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10034 Black-bellied hamster])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5twv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5twv OCA], [https://pdbe.org/5twv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5twv RCSB], [https://www.ebi.ac.uk/pdbsum/5twv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5twv ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == 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] | + | [https://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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </SX> | | </SX> |
| - | [[Category: Black-bellied hamster]] | + | [[Category: Cricetus cricetus]] |
| - | [[Category: Buffalo rat]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chen, J Z]] | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Martin, G M]] | + | [[Category: Chen JZ]] |
| - | [[Category: Shyng, S L]] | + | [[Category: Martin GM]] |
| - | [[Category: Yoshioka, C]] | + | [[Category: Shyng SL]] |
| - | [[Category: Katp]] | + | [[Category: Yoshioka C]] |
| - | [[Category: Kir6 2]]
| + | |
| - | [[Category: Potassium channel]]
| + | |
| - | [[Category: Sur1]]
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| - | [[Category: Transport protein]]
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| 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 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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Martin GM, Yoshioka C, Rex EA, Fay JF, Xie Q, Whorton MR, Chen JZ, Shyng SL. Cryo-EM structure of the ATP-sensitive potassium channel illuminates mechanisms of assembly and gating. Elife. 2017 Jan 16;6. pii: e24149. doi: 10.7554/eLife.24149. PMID:28092267 doi:http://dx.doi.org/10.7554/eLife.24149
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