3oxq

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[[Image:3oxq.png|left|200px]]
 
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==Crystal Structure of Ca2+/CaM-CaV1.2 pre-IQ/IQ domain complex==
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The line below this paragraph, containing "STRUCTURE_3oxq", creates the "Structure Box" on the page.
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<StructureSection load='3oxq' size='340' side='right'caption='[[3oxq]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3oxq]] is a 6 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=3OXQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OXQ 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]] 2.55&#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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{{STRUCTURE_3oxq| PDB=3oxq | SCENE= }}
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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=3oxq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oxq OCA], [https://pdbe.org/3oxq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3oxq RCSB], [https://www.ebi.ac.uk/pdbsum/3oxq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3oxq ProSAT]</span></td></tr>
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</table>
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== Disease ==
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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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== 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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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Interactions between voltage-gated calcium channels (Ca(V)s) and calmodulin (CaM) modulate Ca(V) function. In this study, we report the structure of a Ca(2+)/CaM Ca(V)1.2 C-terminal tail complex that contains two PreIQ helices bridged by two Ca(2+)/CaMs and two Ca(2+)/CaM-IQ domain complexes. Sedimentation equilibrium experiments establish that the complex has a 2:1 Ca(2+)/CaM:C-terminal tail stoichiometry and does not form higher order assemblies. Moreover, subunit-counting experiments demonstrate that in live cell membranes Ca(V)1.2s are monomers. Thus, contrary to previous proposals, the crystallographic dimer lacks physiological relevance. Isothermal titration calorimetry and biochemical experiments show that the two Ca(2+)/CaMs in the complex have different properties. Ca(2+)/CaM bound to the PreIQ C-region is labile, whereas Ca(2+)/CaM bound to the IQ domain is not. Furthermore, neither of lobes of apo-CaM interacts strongly with the PreIQ domain. Electrophysiological studies indicate that the PreIQ C-region has a role in calcium-dependent facilitation. Together, the data show that two Ca(2+)/CaMs can bind the Ca(V)1.2 tail simultaneously and indicate a functional role for Ca(2+)/CaM at the C-region site.
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===Crystal Structure of Ca2+/CaM-CaV1.2 pre-IQ/IQ domain complex===
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Multiple C-terminal tail Ca(2+)/CaMs regulate Ca(V)1.2 function but do not mediate channel dimerization.,Kim EY, Rumpf CH, Van Petegem F, Arant RJ, Findeisen F, Cooley ES, Isacoff EY, Minor DL Jr EMBO J. 2010 Oct 15. PMID:20953164<ref>PMID:20953164</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 3oxq" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 20953164 is the PubMed ID number.
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{{ABSTRACT_PUBMED_20953164}}
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==About this Structure==
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[[3oxq]] is a 6 chain structure of [[Ion channels]] and [[Ion channels (Part II)]] 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=3OXQ OCA].
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==See Also==
==See Also==
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*[[Ion channels]]
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*[[Calmodulin 3D structures|Calmodulin 3D structures]]
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*[[Ion channels (Part II)]]
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*[[Ion channels 3D structures|Ion channels 3D structures]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:20953164</ref><references group="xtra"/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Arant, R.]]
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[[Category: Large Structures]]
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[[Category: Cooley, E S.]]
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[[Category: Arant R]]
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[[Category: Findeisen, F.]]
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[[Category: Cooley ES]]
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[[Category: Isacoff, E Y.]]
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[[Category: Findeisen F]]
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[[Category: Kim, E Y.]]
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[[Category: Isacoff EY]]
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[[Category: Minor, D L.]]
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[[Category: Kim EY]]
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[[Category: Petegem, F Van.]]
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[[Category: Minor DL]]
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[[Category: Rumpf, C H.]]
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[[Category: Rumpf CH]]
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[[Category: Van Petegem F]]

Current revision

Crystal Structure of Ca2+/CaM-CaV1.2 pre-IQ/IQ domain complex

PDB ID 3oxq

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