2jzi

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Current revision (19:07, 29 May 2024) (edit) (undo)
 
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==Structure of Calmodulin complexed with the Calmodulin Binding Domain of Calcineurin==
==Structure of Calmodulin complexed with the Calmodulin Binding Domain of Calcineurin==
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<StructureSection load='2jzi' size='340' side='right'caption='[[2jzi]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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<StructureSection load='2jzi' size='340' side='right'caption='[[2jzi]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2jzi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JZI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JZI FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2jzi]] 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=2JZI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JZI FirstGlance]. <br>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CALM1, CALM, CAM, CAM1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), PPP3CA, CALNA, CNA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Phosphoprotein_phosphatase Phosphoprotein phosphatase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.16 3.1.3.16] </span></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=2jzi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jzi OCA], [https://pdbe.org/2jzi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jzi RCSB], [https://www.ebi.ac.uk/pdbsum/2jzi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jzi 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=2jzi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jzi OCA], [https://pdbe.org/2jzi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jzi RCSB], [https://www.ebi.ac.uk/pdbsum/2jzi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jzi ProSAT]</span></td></tr>
</table>
</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.
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/PP2BA_HUMAN PP2BA_HUMAN]] Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin. Dephosphorylates DNM1L, HSPB1 and SSH1.<ref>PMID:15671020</ref> <ref>PMID:18838687</ref>
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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>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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==See Also==
==See Also==
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*[[Calcineurin 3D structures|Calcineurin 3D structures]]
 
*[[Calmodulin 3D structures|Calmodulin 3D structures]]
*[[Calmodulin 3D structures|Calmodulin 3D structures]]
== References ==
== References ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Phosphoprotein phosphatase]]
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[[Category: Chyan C]]
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[[Category: Chyan, C]]
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[[Category: Huang J]]
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[[Category: Huang, J]]
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[[Category: Irene D]]
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[[Category: Irene, D]]
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[[Category: Lin T]]
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[[Category: Lin, T]]
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[[Category: Acetylation]]
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[[Category: Alternative splicing]]
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[[Category: Calcium binding protein]]
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[[Category: Calmodulin-binding]]
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[[Category: Hydrolase]]
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[[Category: Iron]]
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[[Category: Metal binding protein]]
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[[Category: Metal-binding]]
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[[Category: Methylation]]
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[[Category: Nucleus]]
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[[Category: Phosphoprotein]]
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[[Category: Protein phosphatase]]
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[[Category: Ubl conjugation]]
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[[Category: Zinc]]
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Current revision

Structure of Calmodulin complexed with the Calmodulin Binding Domain of Calcineurin

PDB ID 2jzi

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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