5tj6
From Proteopedia
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<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=5tj6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tj6 OCA], [http://pdbe.org/5tj6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tj6 RCSB], [http://www.ebi.ac.uk/pdbsum/5tj6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tj6 ProSAT]</span></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=5tj6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tj6 OCA], [http://pdbe.org/5tj6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tj6 RCSB], [http://www.ebi.ac.uk/pdbsum/5tj6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tj6 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The Ca2+-activated K+ channel, Slo1, has an unusually large conductance and contains a voltage sensor and multiple chemical sensors. Dual activation by membrane voltage and Ca2+ renders Slo1 central to processes that couple electrical signalling to Ca2+-mediated events such as muscle contraction and neuronal excitability. Here we present the cryo-electron microscopy structure of a full-length Slo1 channel from Aplysia californica in the presence of Ca2+ and Mg2+ at a resolution of 3.5 A. The channel adopts an open conformation. Its voltage-sensor domain adopts a non-domain-swapped attachment to the pore and contacts the cytoplasmic Ca2+-binding domain from a neighbouring subunit. Unique structural features of the Slo1 voltage sensor suggest that it undergoes different conformational changes than other known voltage sensors. The structure reveals the molecular details of three distinct divalent cation-binding sites identified through electrophysiological studies of mutant Slo1 channels. | ||
| + | |||
| + | Cryo-EM structure of the open high-conductance Ca2+-activated K+ channel.,Tao X, Hite RK, MacKinnon R Nature. 2017 Jan 5;541(7635):46-51. doi: 10.1038/nature20608. Epub 2016 Dec 14. PMID:27974795<ref>PMID:27974795</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5tj6" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 07:40, 18 January 2017
Ca2+ bound aplysia Slo1
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