6cno: Difference between revisions
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The entry | ==Cryo-EM structure of the human SK4/calmodulin channel complex in the Ca2+ bound state II== | ||
<StructureSection load='6cno' size='340' side='right' caption='[[6cno]], [[Resolution|resolution]] 4.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6cno]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CNO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CNO FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | |||
[[Category: | <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=6cno FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cno OCA], [http://pdbe.org/6cno PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cno RCSB], [http://www.ebi.ac.uk/pdbsum/6cno PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cno ProSAT]</span></td></tr> | ||
</table> | |||
== Disease == | |||
[[http://www.uniprot.org/uniprot/KCNN4_HUMAN KCNN4_HUMAN]] The disease is caused by mutations affecting the gene represented in this entry. [[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 == | |||
[[http://www.uniprot.org/uniprot/KCNN4_HUMAN KCNN4_HUMAN]] Forms a voltage-independent potassium channel that is activated by intracellular calcium (PubMed:26148990). Activation is followed by membrane hyperpolarization which promotes calcium influx. Required for maximal calcium influx and proliferation during the reactivation of naive T-cells. The channel is blocked by clotrimazole and charybdotoxin but is insensitive to apamin (PubMed:17157250, PubMed:18796614).<ref>PMID:17157250</ref> <ref>PMID:18796614</ref> <ref>PMID:26148990</ref> [[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> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Lee, C H]] | |||
[[Category: MacKinnon, R]] | |||
[[Category: Calmodulin]] | |||
[[Category: Ion channel]] | |||
[[Category: Membrane protein]] | |||
[[Category: Neuroscience]] | |||