2n6a
From Proteopedia
(Difference between revisions)
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==NMR structure of a human calmodulin/connexin-36 peptide hybrid== | ==NMR structure of a human calmodulin/connexin-36 peptide hybrid== | ||
- | <StructureSection load='2n6a' size='340' side='right'caption='[[2n6a | + | <StructureSection load='2n6a' size='340' side='right'caption='[[2n6a]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[2n6a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2n6a]] is a 1 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=2N6A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N6A FirstGlance]. <br> |
</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> | </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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3ewt|3ewt]], [[4djc|4djc]]</div></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=2n6a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n6a OCA], [https://pdbe.org/2n6a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n6a RCSB], [https://www.ebi.ac.uk/pdbsum/2n6a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n6a ProSAT]</span></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=2n6a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n6a OCA], [https://pdbe.org/2n6a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n6a RCSB], [https://www.ebi.ac.uk/pdbsum/2n6a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n6a 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> [https://www.uniprot.org/uniprot/CXD2_HUMAN CXD2_HUMAN] One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. | ||
+ | == References == | ||
+ | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: | + | [[Category: Homo sapiens]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Donaldson | + | [[Category: Donaldson L]] |
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Current revision
NMR structure of a human calmodulin/connexin-36 peptide hybrid
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