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| | <SX load='6o20' size='340' side='right' viewer='molstar' caption='[[6o20]], [[Resolution|resolution]] 3.30Å' scene=''> | | <SX load='6o20' size='340' side='right' viewer='molstar' caption='[[6o20]], [[Resolution|resolution]] 3.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6o20]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin] and [http://en.wikipedia.org/wiki/European_rabbit European rabbit]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6O20 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6O20 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6o20]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6O20 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6O20 FirstGlance]. <br> |
| - | </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></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.3Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Trpv5, Ecac1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9986 European rabbit]), CALM, CAM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 BOVIN])</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></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6o20 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6o20 OCA], [http://pdbe.org/6o20 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6o20 RCSB], [http://www.ebi.ac.uk/pdbsum/6o20 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6o20 ProSAT]</span></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=6o20 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6o20 OCA], [https://pdbe.org/6o20 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6o20 RCSB], [https://www.ebi.ac.uk/pdbsum/6o20 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6o20 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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> [[http://www.uniprot.org/uniprot/CALM_BOVIN CALM_BOVIN]] Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases. Together with CEP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis (By similarity). | + | [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> |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | TRPV5 (transient receptor potential vanilloid 5) is a unique calcium-selective TRP channel essential for calcium homeostasis. Unlike other TRPV channels, TRPV5 and its close homolog, TRPV6, do not exhibit thermosensitivity or ligand-dependent activation but are constitutively open at physiological membrane potentials and modulated by calmodulin (CaM) in a calcium-dependent manner. Here we report high-resolution electron cryomicroscopy structures of truncated and full-length TRPV5 in lipid nanodiscs, as well as of a TRPV5 W583A mutant and TRPV5 in complex with CaM. These structures highlight the mechanism of calcium regulation and reveal a flexible stoichiometry of CaM binding to TRPV5.
| + | |
| | | | |
| - | Structural insight into TRPV5 channel function and modulation.,Dang S, van Goor MK, Asarnow D, Wang Y, Julius D, Cheng Y, van der Wijst J Proc Natl Acad Sci U S A. 2019 Apr 11. pii: 1820323116. doi:, 10.1073/pnas.1820323116. PMID:30975749<ref>PMID:30975749</ref>
| + | ==See Also== |
| - | | + | *[[Calmodulin 3D structures|Calmodulin 3D structures]] |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | *[[Ion channels 3D structures|Ion channels 3D structures]] |
| - | </div>
| + | |
| - | <div class="pdbe-citations 6o20" style="background-color:#fffaf0;"></div>
| + | |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </SX> | | </SX> |
| - | [[Category: Bovin]] | + | [[Category: Bos taurus]] |
| - | [[Category: European rabbit]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Asarnow, D]] | + | [[Category: Oryctolagus cuniculus]] |
| - | [[Category: Cheng, Y]] | + | [[Category: Asarnow D]] |
| - | [[Category: Dang, S]] | + | [[Category: Cheng Y]] |
| - | [[Category: Goor, M K.van]] | + | [[Category: Dang S]] |
| - | [[Category: Julius, D]] | + | [[Category: Julius D]] |
| - | [[Category: Wang, Y]] | + | [[Category: Wang Y]] |
| - | [[Category: Wijst, J van der]] | + | [[Category: Van Goor MK]] |
| - | [[Category: Membrane protein]] | + | [[Category: Van der Wijst J]] |
| - | [[Category: Trp channel]]
| + | |
