1wrz

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(New page: 200px<br /> <applet load="1wrz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wrz, resolution 2.00&Aring;" /> '''Calmodulin complexe...)
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[[Image:1wrz.gif|left|200px]]<br />
 
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<applet load="1wrz" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1wrz, resolution 2.00&Aring;" />
 
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'''Calmodulin complexed with a peptide from a human death-associated protein kinase'''<br />
 
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==About this Structure==
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==Calmodulin complexed with a peptide from a human death-associated protein kinase==
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1WRZ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1WRZ OCA].
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<StructureSection load='1wrz' size='340' side='right'caption='[[1wrz]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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[[Category: Homo sapiens]]
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== Structural highlights ==
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[[Category: Non-specific serine/threonine protein kinase]]
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<table><tr><td colspan='2'>[[1wrz]] 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=1WRZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WRZ FirstGlance]. <br>
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[[Category: Protein complex]]
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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&#8491;</td></tr>
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[[Category: Kursula, P.]]
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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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[[Category: Vahokoski, J.]]
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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=1wrz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wrz OCA], [https://pdbe.org/1wrz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wrz RCSB], [https://www.ebi.ac.uk/pdbsum/1wrz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wrz ProSAT]</span></td></tr>
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[[Category: Wilmanns, M.]]
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</table>
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[[Category: CA]]
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== Disease ==
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[[Category: calmodulin]]
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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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[[Category: protein kinase]]
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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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wr/1wrz_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1wrz ConSurf].
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<div style="clear:both"></div>
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:54:15 2007''
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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: Kursula P]]
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[[Category: Vahokoski J]]
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[[Category: Wilmanns M]]

Current revision

Calmodulin complexed with a peptide from a human death-associated protein kinase

PDB ID 1wrz

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