6feg
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Solution Structure of CaM/Kv7.2-hAB Complex== | |
| - | + | <StructureSection load='6feg' size='340' side='right' caption='[[6feg]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[6feg]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FEG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FEG 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=6feg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6feg OCA], [http://pdbe.org/6feg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6feg RCSB], [http://www.ebi.ac.uk/pdbsum/6feg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6feg ProSAT]</span></td></tr> |
| + | </table> | ||
| + | == Disease == | ||
| + | [[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/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: Bernardo-Seisdedos, G]] | ||
[[Category: Millet, O]] | [[Category: Millet, O]] | ||
| - | [[Category: Bernardo-Seisdedos, G]] | ||
[[Category: Villarroel, A]] | [[Category: Villarroel, A]] | ||
| + | [[Category: Calcium-signalling]] | ||
| + | [[Category: Calmodulin]] | ||
| + | [[Category: Complex]] | ||
| + | [[Category: Metal transport]] | ||
| + | [[Category: Transport]] | ||
| + | [[Category: Voltage-gated potassium channel]] | ||
Revision as of 07:32, 22 February 2018
Solution Structure of CaM/Kv7.2-hAB Complex
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