7l8v
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | ==== | + | ==NMR Structure of half-calcified calmodulin mutant (CaMEF12) bound to the IQ-motif of CaV1.2== |
<StructureSection load='7l8v' size='340' side='right'caption='[[7l8v]]' scene=''> | <StructureSection load='7l8v' size='340' side='right'caption='[[7l8v]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full | + | <table><tr><td colspan='2'>[[7l8v]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7L8V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7L8V FirstGlance]. <br> |
| - | </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=7l8v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7l8v OCA], [https://pdbe.org/7l8v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7l8v RCSB], [https://www.ebi.ac.uk/pdbsum/7l8v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7l8v ProSAT]</span></td></tr> | + | </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=7l8v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7l8v OCA], [https://pdbe.org/7l8v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7l8v RCSB], [https://www.ebi.ac.uk/pdbsum/7l8v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7l8v ProSAT]</span></td></tr> | ||
</table> | </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> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Ames JB]] |
Revision as of 06:38, 8 September 2022
NMR Structure of half-calcified calmodulin mutant (CaMEF12) bound to the IQ-motif of CaV1.2
| |||||||||||
