6e2g

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==Cryo-EM structure of rat TRPV6 in complex with Calmodulin==
==Cryo-EM structure of rat TRPV6 in complex with Calmodulin==
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<StructureSection load='6e2g' size='340' side='right' caption='[[6e2g]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
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<SX load='6e2g' size='340' side='right' viewer='molstar' caption='[[6e2g]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6e2g]] is a 5 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E2G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6E2G FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6e2g]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E2G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6E2G FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.6&#8491;</td></tr>
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<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=6e2g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e2g OCA], [http://pdbe.org/6e2g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6e2g RCSB], [http://www.ebi.ac.uk/pdbsum/6e2g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6e2g ProSAT]</span></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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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6e2g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e2g OCA], [https://pdbe.org/6e2g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6e2g RCSB], [https://www.ebi.ac.uk/pdbsum/6e2g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6e2g ProSAT]</span></td></tr>
</table>
</table>
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== Disease ==
 
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[[http://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 ==
== Function ==
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[[http://www.uniprot.org/uniprot/TRPV6_RAT TRPV6_RAT]] Calcium selective cation channel probably involved in Ca(2+) uptake in various tissues, including Ca(2+) reabsorption in intestine. The channel is activated by low internal calcium level, probably including intracellular calcium store depletion, and the current exhibits an inward rectification. Inactivation includes both, a rapid Ca(2+)-dependent and a slower Ca(2+)-calmodulin-dependent mechanism, the latter may be regulated by phosphorylation. In vitro, is slowly inhibited by Mg(2+) in a voltage-independent manner. Heteromeric assembly with TRPV5 seems to modify channel properties. TRPV5-TRPV6 heteromultimeric concatemers exhibit voltage-dependent gating (By similarity).[UniProtKB:Q91WD2][UniProtKB:Q9H1D0]<ref>PMID:11287959</ref> [[http://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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[https://www.uniprot.org/uniprot/TRPV6_RAT TRPV6_RAT] Calcium selective cation channel probably involved in Ca(2+) uptake in various tissues, including Ca(2+) reabsorption in intestine. The channel is activated by low internal calcium level, probably including intracellular calcium store depletion, and the current exhibits an inward rectification. Inactivation includes both, a rapid Ca(2+)-dependent and a slower Ca(2+)-calmodulin-dependent mechanism, the latter may be regulated by phosphorylation. In vitro, is slowly inhibited by Mg(2+) in a voltage-independent manner. Heteromeric assembly with TRPV5 seems to modify channel properties. TRPV5-TRPV6 heteromultimeric concatemers exhibit voltage-dependent gating (By similarity).[UniProtKB:Q91WD2][UniProtKB:Q9H1D0]<ref>PMID:11287959</ref>
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==See Also==
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*[[Calmodulin 3D structures|Calmodulin 3D structures]]
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*[[Ion channels 3D structures|Ion channels 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
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</StructureSection>
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</SX>
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[[Category: McGoldrick, L L]]
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[[Category: Homo sapiens]]
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[[Category: Singh, A K]]
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[[Category: Large Structures]]
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[[Category: Sobolevsky, A I]]
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[[Category: Rattus norvegicus]]
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[[Category: Calcium channel]]
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[[Category: McGoldrick LL]]
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[[Category: Membrane protein]]
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[[Category: Singh AK]]
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[[Category: Trp channel]]
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[[Category: Sobolevsky AI]]
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[[Category: Trpv6]]
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Current revision

Cryo-EM structure of rat TRPV6 in complex with Calmodulin

6e2g, resolution 3.60Å

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