6dmr

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==Lipid-bound full-length rbTRPV5==
==Lipid-bound full-length rbTRPV5==
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<StructureSection load='6dmr' size='340' side='right' caption='[[6dmr]], [[Resolution|resolution]] 3.90&Aring;' scene=''>
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<SX load='6dmr' size='340' side='right' viewer='molstar' caption='[[6dmr]], [[Resolution|resolution]] 3.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6dmr]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DMR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6DMR FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6dmr]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DMR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6DMR FirstGlance]. <br>
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</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=6dmr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dmr OCA], [http://pdbe.org/6dmr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6dmr RCSB], [http://www.ebi.ac.uk/pdbsum/6dmr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6dmr ProSAT]</span></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]] 3.9&#8491;</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=6dmr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dmr OCA], [https://pdbe.org/6dmr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6dmr RCSB], [https://www.ebi.ac.uk/pdbsum/6dmr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6dmr ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/TRPV5_RABIT TRPV5_RABIT]] Constitutively active calcium selective cation channel thought to be involved in Ca(2+) reabsorption in kidney and intestine (PubMed:12574114). Required for normal Ca(2+) reabsorption in the kidney distal convoluted tubules (By similarity). The channel is activated by low internal calcium level and the current exhibits an inward rectification (By similarity). A Ca(2+)-dependent feedback regulation includes fast channel inactivation and slow current decay (By similarity). Heteromeric assembly with TRPV6 seems to modify channel properties. TRPV5-TRPV6 heteromultimeric concatemers exhibit voltage-dependent gating (PubMed:12574114).[UniProtKB:P69744][UniProtKB:Q9NQA5]<ref>PMID:10085067</ref> <ref>PMID:11035011</ref> <ref>PMID:12574114</ref>
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[https://www.uniprot.org/uniprot/TRPV5_RABIT TRPV5_RABIT] Constitutively active calcium selective cation channel thought to be involved in Ca(2+) reabsorption in kidney and intestine (PubMed:12574114). Required for normal Ca(2+) reabsorption in the kidney distal convoluted tubules (By similarity). The channel is activated by low internal calcium level and the current exhibits an inward rectification (By similarity). A Ca(2+)-dependent feedback regulation includes fast channel inactivation and slow current decay (By similarity). Heteromeric assembly with TRPV6 seems to modify channel properties. TRPV5-TRPV6 heteromultimeric concatemers exhibit voltage-dependent gating (PubMed:12574114).[UniProtKB:P69744][UniProtKB:Q9NQA5]<ref>PMID:10085067</ref> <ref>PMID:11035011</ref> <ref>PMID:12574114</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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TRPV5 is a transient receptor potential channel involved in calcium reabsorption. Here we investigate the interaction of two endogenous modulators with TRPV5. Both phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) and calmodulin (CaM) have been shown to directly bind to TRPV5 and activate or inactivate the channel, respectively. Using cryo-electron microscopy (cryo-EM), we determined TRPV5 structures in the presence of dioctanoyl PI(4,5)P2 and CaM. The PI(4,5)P2 structure reveals a binding site between the N-linker, S4-S5 linker and S6 helix of TRPV5. These interactions with PI(4,5)P2 induce conformational rearrangements in the lower gate, opening the channel. The CaM structure reveals two TRPV5 C-terminal peptides anchoring a single CaM molecule and that calcium inhibition is mediated through a cation-pi interaction between Lys116 on the C-lobe of calcium-activated CaM and Trp583 at the intracellular gate of TRPV5. Overall, this investigation provides insight into the endogenous modulation of TRPV5, which has the potential to guide drug discovery.
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Structural insights on TRPV5 gating by endogenous modulators.,Hughes TET, Pumroy RA, Yazici AT, Kasimova MA, Fluck EC, Huynh KW, Samanta A, Molugu SK, Zhou ZH, Carnevale V, Rohacs T, Moiseenkova-Bell VY Nat Commun. 2018 Oct 10;9(1):4198. doi: 10.1038/s41467-018-06753-6. PMID:30305626<ref>PMID:30305626</ref>
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==See Also==
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*[[Ion channels 3D structures|Ion channels 3D structures]]
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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>
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<div class="pdbe-citations 6dmr" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
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</StructureSection>
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</SX>
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[[Category: Hughes, T E.T]]
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[[Category: Large Structures]]
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[[Category: Moiseenkova-Bell, V Y]]
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[[Category: Oryctolagus cuniculus]]
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[[Category: Pumroy, R A]]
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[[Category: Hughes TET]]
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[[Category: Calcium channel]]
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[[Category: Moiseenkova-Bell VY]]
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[[Category: Full-length]]
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[[Category: Pumroy RA]]
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[[Category: Lipid-bound]]
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[[Category: Transport protein]]
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[[Category: Trpv5]]
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Current revision

Lipid-bound full-length rbTRPV5

6dmr, resolution 3.90Å

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