4q57: Difference between revisions

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New page: '''Unreleased structure''' The entry 4q57 is ON HOLD Authors: Song, J.-G., Kostan, J., Grishkovskaya, I., Djinovic-Carugo, K. Description: Crystal structure of the plectin 1a actin-bin...
 
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'''Unreleased structure'''


The entry 4q57 is ON HOLD
==Crystal structure of the plectin 1a actin-binding domain/N-terminal domain of calmodulin complex==
<StructureSection load='4q57' size='340' side='right'caption='[[4q57]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4q57]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q57 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Q57 FirstGlance]. <br>
</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>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=4q57 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q57 OCA], [https://pdbe.org/4q57 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4q57 RCSB], [https://www.ebi.ac.uk/pdbsum/4q57 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4q57 ProSAT]</span></td></tr>
</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>


Authors: Song, J.-G., Kostan, J., Grishkovskaya, I., Djinovic-Carugo, K.
==See Also==
 
*[[Calmodulin 3D structures|Calmodulin 3D structures]]
Description: Crystal structure of the plectin 1a actin-binding domain/N-terminal domain of calmodulin complex
*[[Plectin|Plectin]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Djinovic-Carugo K]]
[[Category: Grishkovskaya I]]
[[Category: Kostan J]]
[[Category: Song J-G]]
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