6o1n: Difference between revisions
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The | ==Cryo-EM structure of TRPV5 (1-660) in nanodisc== | ||
<StructureSection load='6o1n' size='340' side='right'caption='[[6o1n]], [[Resolution|resolution]] 2.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6o1n]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6O1N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6O1N FirstGlance]. <br> | |||
</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=6o1n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6o1n OCA], [http://pdbe.org/6o1n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6o1n RCSB], [http://www.ebi.ac.uk/pdbsum/6o1n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6o1n ProSAT]</span></td></tr> | |||
</table> | |||
== 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> | |||
<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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6o1n" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Asarnow, D]] | [[Category: Asarnow, D]] | ||
[[Category: Cheng, Y]] | [[Category: Cheng, Y]] | ||
[[Category: Dang, S]] | [[Category: Dang, S]] | ||
[[Category: | [[Category: Goor, M K.van]] | ||
[[Category: Julius, D]] | [[Category: Julius, D]] | ||
[[Category: Wang, Y]] | |||
[[Category: Wijst, J van der]] | |||
[[Category: Ion channel]] | |||
[[Category: Membrane protein]] | |||
[[Category: Trp channel]] | |||
Revision as of 07:03, 24 April 2019
Cryo-EM structure of TRPV5 (1-660) in nanodisc
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