6o1p
From Proteopedia
Cryo-EM structure of full length TRPV5 in nanodisc
Structural highlights
Function[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][1] [2] [3] Publication Abstract from PubMedTRPV5 (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[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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