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==X-RAY STRUCTURE OF A DAP-KINASE CALMODULIN COMPLEX==
==X-RAY STRUCTURE OF A DAP-KINASE CALMODULIN COMPLEX==
<StructureSection load='2x0g' size='340' side='right' caption='[[2x0g]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='2x0g' size='340' side='right'caption='[[2x0g]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2x0g]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X0G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2X0G FirstGlance]. <br>
<table><tr><td colspan='2'>[[2x0g]] 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=2X0G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X0G FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><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]] 2.2&#8491;</td></tr>
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2f3z|2f3z]], [[1j7p|1j7p]], [[1nkf|1nkf]], [[1k93|1k93]], [[1xfv|1xfv]], [[1sk6|1sk6]], [[1y6w|1y6w]], [[1iwq|1iwq]], [[1jkl|1jkl]], [[1k90|1k90]], [[1yrt|1yrt]], [[1cll|1cll]], [[1lvc|1lvc]], [[2w73|2w73]], [[1cdl|1cdl]], [[1jkt|1jkt]], [[1xfy|1xfy]], [[1xfu|1xfu]], [[2f3y|2f3y]], [[1xfx|1xfx]], [[1jks|1jks]], [[1s26|1s26]], [[1j7o|1j7o]], [[1ctr|1ctr]], [[1jkk|1jkk]], [[2w4j|2w4j]], [[2w4k|2w4k]], [[1yru|1yru]], [[1wrz|1wrz]], [[2wel|2wel]], [[2v02|2v02]], [[1xfz|1xfz]], [[1p4f|1p4f]], [[1pk0|1pk0]], [[2v01|2v01]], [[1xfw|1xfw]], [[2be6|2be6]], [[1ig1|1ig1]], [[1zot|1zot]], [[1sw8|1sw8]], [[2vay|2vay]], [[1aji|1aji]]</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=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </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=2x0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x0g OCA], [https://pdbe.org/2x0g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2x0g RCSB], [https://www.ebi.ac.uk/pdbsum/2x0g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2x0g ProSAT]</span></td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2x0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x0g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2x0g RCSB], [http://www.ebi.ac.uk/pdbsum/2x0g PDBsum]</span></td></tr>
</table>
<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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/x0/2x0g_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/x0/2x0g_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
</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/chain_selection.php?pdb_ID=2ata ConSurf].
</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=2x0g ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 2x0g" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Calmodulin|Calmodulin]]
*[[Calcium/calmodulin dependent protein kinase 3D structures|Calcium/calmodulin dependent protein kinase 3D structures]]
*[[Death-associated protein kinase|Death-associated protein kinase]]
*[[Calmodulin 3D structures|Calmodulin 3D structures]]
*[[Death-associated protein kinase 3D structures|Death-associated protein kinase 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Non-specific serine/threonine protein kinase]]
[[Category: Large Structures]]
[[Category: Diego, I De.]]
[[Category: De Diego I]]
[[Category: Kuper, J.]]
[[Category: Kuper J]]
[[Category: Lehmann, F.]]
[[Category: Lehmann F]]
[[Category: Wilmanns, M.]]
[[Category: Wilmanns M]]
[[Category: Ank repeat]]
[[Category: Atp-binding]]
[[Category: Calmodulin]]
[[Category: Calmodulin-binding]]
[[Category: Dapk]]
[[Category: Kinase]]
[[Category: Phosphoprotein]]
[[Category: Transferase]]
[[Category: Transferase signaling protein complex]]
[[Category: Transferase-signaling protein complex]]

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