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The | ==Cryo-EM structure of human TRPV6 in complex with (4- phenylcyclohexyl)piperazine inhibitor 3OG== | ||
<StructureSection load='7k4d' size='340' side='right'caption='[[7k4d]], [[Resolution|resolution]] 3.66Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7k4d]] is a 4 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=7K4D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7K4D FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.66Å</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=VUM:5-[(4-{trans-4-hydroxy-4-[3-(trifluoromethyl)phenyl]cyclohexyl}piperazin-1-yl)methyl]pyridin-2(1H)-one'>VUM</scene></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=7k4d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7k4d OCA], [https://pdbe.org/7k4d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7k4d RCSB], [https://www.ebi.ac.uk/pdbsum/7k4d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7k4d ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://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> | |||
==See Also== | |||
*[[Ion channels 3D structures|Ion channels 3D structures]] | |||
== References == | |||
[[Category: | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Nadezhdin KD]] | |||
[[Category: Neuberger A]] | |||
[[Category: Singh AK]] | |||
[[Category: Sobolevsky AI]] | |||
Latest revision as of 17:55, 6 March 2024
Cryo-EM structure of human TRPV6 in complex with (4- phenylcyclohexyl)piperazine inhibitor 3OGCryo-EM structure of human TRPV6 in complex with (4- phenylcyclohexyl)piperazine inhibitor 3OG
Structural highlights
FunctionTRPV6_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][1] [2] [3] [4] [5] See AlsoReferences
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