2k0f

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{{Large structure}}
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==Calmodulin complexed with calmodulin-binding peptide from smooth muscle myosin light chain kinase==
==Calmodulin complexed with calmodulin-binding peptide from smooth muscle myosin light chain kinase==
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<StructureSection load='2k0f' size='340' side='right' caption='[[2k0f]], [[NMR_Ensembles_of_Models | 160 NMR models]]' scene=''>
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<StructureSection load='2k0f' size='340' side='right'caption='[[2k0f]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2k0f]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K0F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2K0F FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2k0f]] 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=2K0F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2K0F 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">Solution NMR</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1cdl|1cdl]], [[2k0e|2k0e]]</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CALM1, CALM, CAM, CAM1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=2k0f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k0f OCA], [https://pdbe.org/2k0f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k0f RCSB], [https://www.ebi.ac.uk/pdbsum/2k0f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k0f 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=2k0f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k0f OCA], [http://pdbe.org/2k0f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2k0f RCSB], [http://www.ebi.ac.uk/pdbsum/2k0f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2k0f ProSAT]</span></td></tr>
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</table>
</table>
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{{Large structure}}
 
== Disease ==
== Disease ==
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[[http://www.uniprot.org/uniprot/MYLK_HUMAN MYLK_HUMAN]] Defects in MYLK are the cause of familial aortic aneurysm thoracic type 7 (AAT7) [MIM:[http://omim.org/entry/613780 613780]]. AAT7 is a disease characterized by permanent dilation of the thoracic aorta usually due to degenerative changes in the aortic wall. It is primarily associated with a characteristic histologic appearance known as 'medial necrosis' or 'Erdheim cystic medial necrosis' in which there is degeneration and fragmentation of elastic fibers, loss of smooth muscle cells, and an accumulation of basophilic ground substance.<ref>PMID:21055718</ref>
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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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[[http://www.uniprot.org/uniprot/MYLK_HUMAN MYLK_HUMAN]] Calcium/calmodulin-dependent myosin light chain kinase implicated in smooth muscle contraction via phosphorylation of myosin light chains (MLC). Also regulates actin-myosin interaction through a non-kinase activity. Phosphorylates PTK2B/PYK2 and myosin light-chains. Involved in the inflammatory response (e.g. apoptosis, vascular permeability, leukocyte diapedesis), cell motility and morphology, airway hyperreactivity and other activities relevant to asthma. Required for tonic airway smooth muscle contraction that is necessary for physiological and asthmatic airway resistance. Necessary for gastrointestinal motility. Implicated in the regulation of endothelial as well as vascular permeability, probably via the regulation of cytoskeletal rearrangements. In the nervous system it has been shown to control the growth initiation of astrocytic processes in culture and to participate in transmitter release at synapses formed between cultured sympathetic ganglion cells. Critical participant in signaling sequences that result in fibroblast apoptosis. Plays a role in the regulation of epithelial cell survival. Required for epithelial wound healing, especially during actomyosin ring contraction during purse-string wound closure. Mediates RhoA-dependent membrane blebbing. Triggers TRPC5 channel activity in a calcium-dependent signaling, by inducing its subcellular localization at the plasma membrane. Promotes cell migration (including tumor cells) and tumor metastasis. PTK2B/PYK2 activation by phosphorylation mediates ITGB2 activation and is thus essential to trigger neutrophil transmigration during acute lung injury (ALI). May regulate optic nerve head astrocyte migration. Probably involved in mitotic cytoskeletal regulation. Regulates tight junction probably by modulating ZO-1 exchange in the perijunctional actomyosin ring. Mediates burn-induced microvascular barrier injury; triggers endothelial contraction in the development of microvascular hyperpermeability by phosphorylating MLC. Essential for intestinal barrier dysfunction. Mediates Giardia spp.-mediated reduced epithelial barrier function during giardiasis intestinal infection via reorganization of cytoskeletal F-actin and tight junctional ZO-1. Necessary for hypotonicity-induced Ca(2+) entry and subsequent activation of volume-sensitive organic osmolyte/anion channels (VSOAC) in cervical cancer cells. Responsible for high proliferative ability of breast cancer cells through anti-apoptosis.<ref>PMID:11113114</ref> <ref>PMID:15020676</ref> <ref>PMID:11976941</ref> <ref>PMID:15825080</ref> <ref>PMID:16723733</ref> <ref>PMID:16284075</ref> <ref>PMID:18710790</ref> <ref>PMID:18587400</ref> <ref>PMID:19826488</ref> <ref>PMID:20453870</ref> <ref>PMID:20375339</ref> <ref>PMID:20181817</ref> <ref>PMID:20139351</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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*[[Calmodulin|Calmodulin]]
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*[[Calmodulin 3D structures|Calmodulin 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Bui, J M]]
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[[Category: Large Structures]]
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[[Category: Cavalli, A]]
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[[Category: Bui JM]]
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[[Category: Christodoulou, J]]
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[[Category: Cavalli A]]
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[[Category: Dobson, C M]]
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[[Category: Christodoulou J]]
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[[Category: Gsponer, J]]
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[[Category: Dobson CM]]
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[[Category: Richter, B]]
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[[Category: Gsponer J]]
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[[Category: Vendruscolo, M]]
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[[Category: Richter B]]
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[[Category: Calcium binding]]
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[[Category: Vendruscolo M]]
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[[Category: Ef hand]]
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[[Category: Ensemble]]
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[[Category: Helix bundle]]
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[[Category: Metal binding protein]]
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Current revision

Calmodulin complexed with calmodulin-binding peptide from smooth muscle myosin light chain kinase

PDB ID 2k0f

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