2y4v

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==CRYSTAL STRUCTURE OF HUMAN CALMODULIN IN COMPLEX WITH A DAP KINASE-1 MUTANT (W305Y) PEPTIDE==
==CRYSTAL STRUCTURE OF HUMAN CALMODULIN IN COMPLEX WITH A DAP KINASE-1 MUTANT (W305Y) PEPTIDE==
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<StructureSection load='2y4v' size='340' side='right' caption='[[2y4v]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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<StructureSection load='2y4v' size='340' side='right'caption='[[2y4v]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2y4v]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y4V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2Y4V FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2y4v]] 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=2Y4V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Y4V FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1j7p|1j7p]], [[2f3z|2f3z]], [[1nkf|1nkf]], [[2x0g|2x0g]], [[1k93|1k93]], [[1xfv|1xfv]], [[1sk6|1sk6]], [[1y6w|1y6w]], [[1jkl|1jkl]], [[1iwq|1iwq]], [[1k90|1k90]], [[1yrt|1yrt]], [[2w73|2w73]], [[1cll|1cll]], [[1lvc|1lvc]], [[1cdl|1cdl]], [[1jkt|1jkt]], [[1xfu|1xfu]], [[1xfy|1xfy]], [[2f3y|2f3y]], [[1jks|1jks]], [[1xfx|1xfx]], [[1s26|1s26]], [[1j7o|1j7o]], [[1jkk|1jkk]], [[1ctr|1ctr]], [[2y0a|2y0a]], [[2w4j|2w4j]], [[2w4k|2w4k]], [[1yru|1yru]], [[1wrz|1wrz]], [[2xzs|2xzs]], [[2wel|2wel]], [[2v02|2v02]], [[1p4f|1p4f]], [[1xfz|1xfz]], [[2v01|2v01]], [[1xfw|1xfw]], [[1pk0|1pk0]], [[2be6|2be6]], [[1ig1|1ig1]], [[2vay|2vay]], [[1sw8|1sw8]], [[1zot|1zot]], [[2xuu|2xuu]], [[1aji|1aji]], [[2y4p|2y4p]]</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'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </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=2y4v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y4v OCA], [https://pdbe.org/2y4v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2y4v RCSB], [https://www.ebi.ac.uk/pdbsum/2y4v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2y4v ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2y4v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y4v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2y4v RCSB], [http://www.ebi.ac.uk/pdbsum/2y4v PDBsum]</span></td></tr>
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</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.
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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>
==See Also==
==See Also==
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*[[Calmodulin|Calmodulin]]
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*[[Calmodulin 3D structures|Calmodulin 3D structures]]
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Non-specific serine/threonine protein kinase]]
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[[Category: Large Structures]]
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[[Category: Diego, I De.]]
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[[Category: Lehmann F]]
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[[Category: Lehmann, F.]]
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[[Category: Wilmanns M]]
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[[Category: Wilmanns, M.]]
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[[Category: De Diego I]]
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[[Category: Metal binding protein-transferase complex]]
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Current revision

CRYSTAL STRUCTURE OF HUMAN CALMODULIN IN COMPLEX WITH A DAP KINASE-1 MUTANT (W305Y) PEPTIDE

PDB ID 2y4v

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