6os4
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | The entry | + | ==Calmodulin in complex with farnesyl cysteine methyl ester== |
| - | + | <StructureSection load='6os4' size='340' side='right'caption='[[6os4]], [[Resolution|resolution]] 2.05Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[6os4]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OS4 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6OS4 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5U0:s-farnesyl-l-cysteine+methyl+ester'>5U0</scene>, <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://proteopedia.org/fgij/fg.htm?mol=6os4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6os4 OCA], [http://pdbe.org/6os4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6os4 RCSB], [http://www.ebi.ac.uk/pdbsum/6os4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6os4 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: Large Structures]] | ||
| + | [[Category: Back, S I]] | ||
| + | [[Category: Enomoto, M]] | ||
| + | [[Category: Gebregiworgis, T]] | ||
| + | [[Category: Grant, B M.M]] | ||
| + | [[Category: Ikura, M]] | ||
| + | [[Category: Ishiyama, N]] | ||
| + | [[Category: Lee, K Y]] | ||
| + | [[Category: Marshall, C]] | ||
| + | [[Category: Complex]] | ||
| + | [[Category: Lipid]] | ||
| + | [[Category: Metal binding protein]] | ||
| + | [[Category: Translocation]] | ||
Revision as of 06:50, 8 April 2020
Calmodulin in complex with farnesyl cysteine methyl ester
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