4bw7: Difference between revisions

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<StructureSection load='4bw7' size='340' side='right'caption='[[4bw7]], [[Resolution|resolution]] 1.81&Aring;' scene=''>
<StructureSection load='4bw7' size='340' side='right'caption='[[4bw7]], [[Resolution|resolution]] 1.81&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4bw7]] is a 2 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=4BW7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BW7 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4bw7]] 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=4BW7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BW7 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SR:STRONTIUM+ION'>SR</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SR:STRONTIUM+ION'>SR</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4bw8|4bw8]]</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=4bw7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bw7 OCA], [https://pdbe.org/4bw7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bw7 RCSB], [https://www.ebi.ac.uk/pdbsum/4bw7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bw7 ProSAT]</span></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=4bw7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bw7 OCA], [http://pdbe.org/4bw7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4bw7 RCSB], [http://www.ebi.ac.uk/pdbsum/4bw7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4bw7 ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Disease ==
== Publication Abstract from PubMed ==
[[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.
Calmodulin is one of the most well characterized proteins and a widely used model system for calcium binding and large-scale protein conformational changes. Its long central helix is usually cut in half when a target peptide is bound. Here, two new crystal structures of calmodulin are presented, in which conformations possibly representing the first steps of calmodulin conformational collapse have been trapped. The central helix in the two structures is bent in the middle, causing a significant movement of the N- and C-terminal lobes with respect to one another. In both of the bent structures, a nearby polar side chain is inserted into the helical groove, disrupting backbone hydrogen bonding. The structures give an insight into the details of the factors that may be involved in the distortion of the central helix upon ligand peptide binding.
== 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>  
Crystallographic snapshots of initial steps in the collapse of the calmodulin central helix.,Kursula P Acta Crystallogr D Biol Crystallogr. 2014 Jan;70(Pt 1):24-30. doi:, 10.1107/S1399004713024437. Epub 2013 Dec 24. PMID:24419375<ref>PMID:24419375</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4bw7" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Kursula, P]]
[[Category: Kursula P]]
[[Category: Metal binding protein]]

Revision as of 17:12, 7 September 2022

Calmodulin in complex with strontium

4bw7, resolution 1.81Å

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