5dbr: Difference between revisions
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New page: '''Unreleased structure''' The entry 5dbr is ON HOLD until Paper Publication Authors: Johnson, C.N., Thompson, M.K., Chazin, W.J. Description: Ca2+ CaM with human cardiac Na+ channel (... |
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The entry | ==Ca2+ CaM with human cardiac Na+ channel (NaV1.5) inactivation gate== | ||
<StructureSection load='5dbr' size='340' side='right'caption='[[5dbr]], [[Resolution|resolution]] 2.25Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5dbr]] 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=5DBR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DBR 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]] 2.25Å</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=5dbr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dbr OCA], [https://pdbe.org/5dbr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dbr RCSB], [https://www.ebi.ac.uk/pdbsum/5dbr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dbr ProSAT]</span></td></tr> | |||
</table> | |||
== Disease == | |||
[https://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 == | |||
[https://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> | |||
==See Also== | |||
*[[Calmodulin 3D structures|Calmodulin 3D structures]] | |||
*[[Ion channels 3D structures|Ion channels 3D structures]] | |||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Chazin WJ]] | |||
[[Category: Johnson CN]] | |||
[[Category: Thompson MK]] | |||
Latest revision as of 08:45, 27 September 2023
Ca2+ CaM with human cardiac Na+ channel (NaV1.5) inactivation gate
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