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6pby

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==Single particle cryo-EM structure of the voltage-gated K+ channel Eag1 3-13 deletion mutant bound to calmodulin (conformation 1)==
==Single particle cryo-EM structure of the voltage-gated K+ channel Eag1 3-13 deletion mutant bound to calmodulin (conformation 1)==
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<StructureSection load='6pby' size='340' side='right'caption='[[6pby]], [[Resolution|resolution]] 3.67&Aring;' scene=''>
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<SX load='6pby' size='340' side='right' viewer='molstar' caption='[[6pby]], [[Resolution|resolution]] 3.67&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6pby]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PBY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6PBY FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6pby]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] 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=6PBY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6PBY FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Kcnh1, Eag ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat]), CALM1, CALM, CAM, CAM1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.67&#8491;</td></tr>
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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=6pby FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pby OCA], [http://pdbe.org/6pby PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6pby RCSB], [http://www.ebi.ac.uk/pdbsum/6pby PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6pby ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6pby FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pby OCA], [https://pdbe.org/6pby PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6pby RCSB], [https://www.ebi.ac.uk/pdbsum/6pby PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6pby ProSAT]</span></td></tr>
</table>
</table>
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== Disease ==
 
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[[http://www.uniprot.org/uniprot/CALM1_HUMAN CALM1_HUMAN]] The disease is caused by mutations affecting the gene represented in this entry. Mutations in CALM1 are the cause of CPVT4. The disease is caused by mutations affecting the gene represented in this entry. Mutations in CALM1 are the cause of LQT14.
 
== Function ==
== Function ==
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[[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] [[http://www.uniprot.org/uniprot/CALM1_HUMAN CALM1_HUMAN]] Calmodulin mediates the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Among the enzymes to be stimulated by the calmodulin-calcium complex are a number of protein kinases and phosphatases. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis (PubMed:16760425). Mediates calcium-dependent inactivation of CACNA1C (PubMed:26969752). Positively regulates calcium-activated potassium channel activity of KCNN2 (PubMed:27165696).<ref>PMID:16760425</ref> <ref>PMID:23893133</ref> <ref>PMID:26969752</ref> <ref>PMID:27165696</ref>
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[https://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]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Voltage-gated potassium channels (Kvs) are gated by transmembrane voltage sensors (VS) that move in response to changes in membrane voltage. Kv10.1 or Eag1 also has three intracellular domains: PAS, C-linker, and CNBHD. We demonstrate that the Eag1 intracellular domains are not required for voltage-dependent gating but likely interact with the VS to modulate gating. We identified specific interactions between the PAS, CNBHD, and VS that modulate voltage-dependent gating and provide evidence that VS movement destabilizes these interactions to promote channel opening. Additionally, mutation of these interactions renders Eag1 insensitive to calmodulin inhibition. The structure of the calmodulin insensitive mutant in a pre-open conformation suggests that channel opening may occur through a rotation of the intracellular domains and calmodulin may prevent this rotation by stabilizing interactions between the VS and intracellular domains. Intracellular domains likely play a similar modulatory role in voltage-dependent gating of the related Kv11-12 channels.
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Regulation of Eag1 gating by its intracellular domains.,Whicher JR, MacKinnon R Elife. 2019 Sep 6;8. pii: 49188. doi: 10.7554/eLife.49188. PMID:31490124<ref>PMID:31490124</ref>
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==See Also==
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*[[Calmodulin 3D structures|Calmodulin 3D structures]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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*[[Potassium channel 3D structures|Potassium channel 3D structures]]
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</div>
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<div class="pdbe-citations 6pby" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
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</StructureSection>
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</SX>
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[[Category: Buffalo rat]]
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[[Category: Homo sapiens]]
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[[Category: Human]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: MacKinnon, R]]
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[[Category: Rattus norvegicus]]
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[[Category: Whicher, J R]]
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[[Category: MacKinnon R]]
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[[Category: Calmodulin]]
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[[Category: Whicher JR]]
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[[Category: Ion channel]]
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[[Category: Transport protein-calcium binding protein complex]]
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[[Category: Voltage-gated potassium channel]]
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Current revision

Single particle cryo-EM structure of the voltage-gated K+ channel Eag1 3-13 deletion mutant bound to calmodulin (conformation 1)

6pby, resolution 3.67Å

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