6sz5

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(New page: '''Unreleased structure''' The entry 6sz5 is ON HOLD Authors: Millana, E., Mattevi, A. Description: Human calmodulin bound to a peptide of human NADPH oxidase 5 [[Category: Unreleased ...)
Current revision (12:50, 24 January 2024) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 6sz5 is ON HOLD
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==Human calmodulin bound to a peptide of human NADPH oxidase 5==
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<StructureSection load='6sz5' size='340' side='right'caption='[[6sz5]], [[Resolution|resolution]] 2.23&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6sz5]] is a 3 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=6SZ5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SZ5 FirstGlance]. <br>
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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]] 2.23&#8491;</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6sz5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sz5 OCA], [https://pdbe.org/6sz5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6sz5 RCSB], [https://www.ebi.ac.uk/pdbsum/6sz5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6sz5 ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/CALM2_HUMAN CALM2_HUMAN] Catecholaminergic polymorphic ventricular tachycardia;Brugada syndrome;Romano-Ward syndrome. The disease is caused by mutations affecting the gene represented in this entry. Mutations in CALM2 are the cause of LQT15.
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== Function ==
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[https://www.uniprot.org/uniprot/CALM2_HUMAN CALM2_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:26969752</ref> <ref>PMID:27165696</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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It is now accepted that Reactive Oxygen Species (ROS) are not only dangerous oxidative agents but also chemical mediators of the redox cell signaling and innate immune response. A central role in ROS controlled production is played by the NADPH oxidases (NOXs), a group of seven membrane-bound enzymes (NOX1-5 and DUOX1-2) whose unique function is to produce ROS. Here, we describe the regulation of NOX5, a widespread family-member present in cyanobacteria, protists, plants, fungi and the animal kingdom. We show that the calmodulin-like regulatory EF-domain of NOX5 is partially unfolded and detached from the rest of the protein in the absence of calcium. In the presence of calcium, the C-terminal lobe of the EF-domain acquires an ordered and more compact structure that enables its binding to the enzyme dehydrogenase domain. Our spectroscopic and mutagenesis studies further identified a set of conserved aspartate residues in the dehydrogenase domain that are essential for NOX5 activation. Altogether, our work shows that calcium induces an unfolded-to-folded transition of the EF-domain that promotes direct interaction with a conserved regulatory region, resulting in NOX5 activation.
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Authors: Millana, E., Mattevi, A.
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On the mechanism of calcium-dependent activation of NADPH oxidase 5 (NOX5).,Millana-Fananas E, Todesca S, Siccorello A, Masino L, Pompach P, Magnani F, Pastore A, Mattevi A FEBS J. 2019 Nov 30. doi: 10.1111/febs.15160. PMID:31785178<ref>PMID:31785178</ref>
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Description: Human calmodulin bound to a peptide of human NADPH oxidase 5
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Mattevi, A]]
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<div class="pdbe-citations 6sz5" style="background-color:#fffaf0;"></div>
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[[Category: Millana, E]]
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==See Also==
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*[[Calmodulin 3D structures|Calmodulin 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Mattevi A]]
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[[Category: Millana E]]

Current revision

Human calmodulin bound to a peptide of human NADPH oxidase 5

PDB ID 6sz5

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