2v02: Difference between revisions

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OCA

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-==RECOMBINANT VERTEBRATE CALMODULIN COMPLEXED WITH BA==
-<StructureSection load='2v02' size='340' side='right' caption='[[2v02]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
+==Recombinant vertebrate calmodulin complexed with Ba==
+<StructureSection load='2v02' size='340' side='right'caption='[[2v02]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2v02]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V02 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2V02 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2v02]] is a 1 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=2V02 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V02 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BA:BARIUM+ION'>BA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1aji|1aji]], [[1cdl|1cdl]], [[1cll|1cll]], [[1ctr|1ctr]], [[1iwq|1iwq]], [[1j7o|1j7o]], [[1j7p|1j7p]], [[1k90|1k90]], [[1k93|1k93]], [[1l7z|1l7z]], [[1lvc|1lvc]], [[1nkf|1nkf]], [[1pk0|1pk0]], [[1s26|1s26]], [[1sk6|1sk6]], [[1sw8|1sw8]], [[1wrz|1wrz]], [[1xfu|1xfu]], [[1xfv|1xfv]], [[1xfw|1xfw]], [[1xfx|1xfx]], [[1xfy|1xfy]], [[1xfz|1xfz]], [[1y6w|1y6w]], [[1yr5|1yr5]], [[1yrt|1yrt]], [[1yru|1yru]], [[1zot|1zot]], [[2be6|2be6]], [[2f3y|2f3y]], [[2f3z|2f3z]], [[2v01|2v01]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BA:BARIUM+ION'>BA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
-<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=2v02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v02 OCA], [http://pdbe.org/2v02 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2v02 RCSB], [http://www.ebi.ac.uk/pdbsum/2v02 PDBsum]</span></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=2v02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v02 OCA], [https://pdbe.org/2v02 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v02 RCSB], [https://www.ebi.ac.uk/pdbsum/2v02 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v02 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>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
    <jmolCheckbox>
-     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v0/2v02_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v0/2v02_consurf.spt"</scriptWhenChecked>
      <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
      <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 28: / Line 33: @@
 ==See Also==
-*[[Calmodulin|Calmodulin]]
+*[[Calmodulin 3D structures|Calmodulin 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
-[[Category: Kursula, P]]
+[[Category: Large Structures]]
-[[Category: Majava, V]]
+[[Category: Kursula P]]
-[[Category: Metal-binding protein]]
+[[Category: Majava V]]
-[[Category: Methylation]]
-[[Category: Phosphorylation]]