5k7l
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Single particle cryo-EM structure of the voltage-gated K+ channel Eag1 bound to the channel inhibitor calmodulin== | |
| + | <StructureSection load='5k7l' size='340' side='right' caption='[[5k7l]], [[Resolution|resolution]] 3.78Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5k7l]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K7L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5K7L FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5k7l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k7l OCA], [http://pdbe.org/5k7l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5k7l RCSB], [http://www.ebi.ac.uk/pdbsum/5k7l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5k7l ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/KCNH1_RAT KCNH1_RAT]] Pore-forming (alpha) subunit of a voltage-gated delayed rectifier potassium channel. Channel properties may be modulated by subunit assembly, but not by cyclic nucleotides (By similarity). Mediates IK(NI) current in myoblasts (By similarity). Involved in the regulation of cell proliferation and differentiation, as adipogenic and osteogenic differentiation in bone marrow-derived mesenchymal stem cells (MSCs) (By similarity).[UniProtKB:O95259][UniProtKB:Q60603] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Voltage-gated potassium (K(v)) channels are gated by the movement of the transmembrane voltage sensor, which is coupled, through the helical S4-S5 linker, to the potassium pore. We determined the single-particle cryo-electron microscopy structure of mammalian K(v)10.1, or Eag1, bound to the channel inhibitor calmodulin, at 3.78 angstrom resolution. Unlike previous K(v) structures, the S4-S5 linker of Eag1 is a five-residue loop and the transmembrane segments are not domain swapped, which suggest an alternative mechanism of voltage-dependent gating. Additionally, the structure and position of the S4-S5 linker allow calmodulin to bind to the intracellular domains and to close the potassium pore, independent of voltage-sensor position. The structure reveals an alternative gating mechanism for K(v) channels and provides a template to further understand the gating properties of Eag1 and related channels. | ||
| - | + | Structure of the voltage-gated K(+) channel Eag1 reveals an alternative voltage sensing mechanism.,Whicher JR, MacKinnon R Science. 2016 Aug 12;353(6300):664-9. doi: 10.1126/science.aaf8070. PMID:27516594<ref>PMID:27516594</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5k7l" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: MacKinnon, R]] | ||
| + | [[Category: Whicher, J R]] | ||
| + | [[Category: Calmodulin]] | ||
| + | [[Category: Cryoelectron microscopy]] | ||
| + | [[Category: Eag1]] | ||
| + | [[Category: Metal transport-calcium binding protein complex]] | ||
| + | [[Category: Voltage-gated potassium channel]] | ||
Revision as of 04:33, 9 September 2016
Single particle cryo-EM structure of the voltage-gated K+ channel Eag1 bound to the channel inhibitor calmodulin
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