6e2f
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | The entry | + | ==Cryo-EM structure of human TRPV6 in complex with Calmodulin== |
| - | + | <StructureSection load='6e2f' size='340' side='right' caption='[[6e2f]], [[Resolution|resolution]] 3.90Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[6e2f]] is a 5 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E2F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6E2F FirstGlance]. <br> | |
| - | + | </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> | |
| - | [[Category: | + | <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=6e2f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e2f OCA], [http://pdbe.org/6e2f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6e2f RCSB], [http://www.ebi.ac.uk/pdbsum/6e2f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6e2f ProSAT]</span></td></tr> |
| + | </table> | ||
| + | == Disease == | ||
| + | [[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 == | ||
| + | [[http://www.uniprot.org/uniprot/TRPV6_HUMAN TRPV6_HUMAN]] Calcium selective cation channel that mediates Ca(2+) uptake in various tissues, including the intestine (PubMed:11097838, PubMed:11278579, PubMed:11248124 PubMed:15184369, PubMed:23612980). Important for normal Ca(2+) ion homeostasis in the body, including bone and skin (By similarity). The channel is activated by low internal calcium level, probably including intracellular calcium store depletion, and the current exhibits an inward rectification (PubMed:15184369). 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.[UniProtKB:Q91WD2]<ref>PMID:11097838</ref> <ref>PMID:11248124</ref> <ref>PMID:11278579</ref> <ref>PMID:15184369</ref> <ref>PMID:23612980</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> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: McGoldrick, L L]] | ||
| + | [[Category: Singh, A K]] | ||
| + | [[Category: Sobolevsky, A I]] | ||
| + | [[Category: Calcium channel]] | ||
| + | [[Category: Membrane protein]] | ||
| + | [[Category: Trp channel]] | ||
| + | [[Category: Trpv6]] | ||
Revision as of 06:09, 22 August 2018
Cryo-EM structure of human TRPV6 in complex with Calmodulin
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