7vuo

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'''Unreleased structure'''
 
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The entry 7vuo is ON HOLD until Paper Publication
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==Crystal Structure of the Kv7.1 C-terminal Domain in Complex with Calmodulin disease mutation F141L==
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<StructureSection load='7vuo' size='340' side='right'caption='[[7vuo]], [[Resolution|resolution]] 2.68&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[7vuo]] 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=7VUO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7VUO FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.679&#8491;</td></tr>
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<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>
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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=7vuo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7vuo OCA], [https://pdbe.org/7vuo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7vuo RCSB], [https://www.ebi.ac.uk/pdbsum/7vuo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7vuo ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[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.
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== Function ==
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[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>
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Authors:
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==See Also==
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*[[Calmodulin 3D structures|Calmodulin 3D structures]]
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Description:
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== References ==
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[[Category: Unreleased Structures]]
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Chen L]]

Current revision

Crystal Structure of the Kv7.1 C-terminal Domain in Complex with Calmodulin disease mutation F141L

PDB ID 7vuo

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