6mud
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | The entry | + | ==Voltage-gated sodium channel NaV1.5 C-terminal domain in complex with Ca2+/Calmodulin== |
| + | <StructureSection load='6mud' size='340' side='right'caption='[[6mud]], [[Resolution|resolution]] 2.69Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6mud]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MUD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MUD FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.69Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6mud FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mud OCA], [https://pdbe.org/6mud PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mud RCSB], [https://www.ebi.ac.uk/pdbsum/6mud PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6mud ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Disease == | ||
| + | [https://www.uniprot.org/uniprot/CALM2_HUMAN CALM2_HUMAN] Catecholaminergic polymorphic ventricular tachycardia;Brugada syndrome;Romano-Ward syndrome. The disease is caused by mutations affecting the gene represented in this entry. Mutations in CALM2 are the cause of LQT15. | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/CALM2_HUMAN CALM2_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:26969752</ref> <ref>PMID:27165696</ref> | ||
| - | + | ==See Also== | |
| - | + | *[[Calmodulin 3D structures|Calmodulin 3D structures]] | |
| - | + | *[[Ion channels 3D structures|Ion channels 3D structures]] | |
| - | [[Category: | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Gardill BR]] | ||
| + | [[Category: Tung CC]] | ||
| + | [[Category: Van Petegem F]] | ||
Current revision
Voltage-gated sodium channel NaV1.5 C-terminal domain in complex with Ca2+/Calmodulin
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