6O20

Cryo-EM structure of TRPV5 with calmodulin bound

Summary for 6O20

• Entry DOI: 10.2210/pdb6o20/pdb
• EMDB information: 0593 0594 0605 0607
• Descriptor: Transient receptor potential cation channel subfamily V member 5, Calmodulin, CALCIUM ION (3 entities in total)
• Functional Keywords: trp channel, membrane protein
• Biological source: Oryctolagus cuniculus (Rabbit); More
• Total number of polymer chains: 6
• Total formula weight: 433682.50

Authors

Dang, S.,van Goor, M.K.,Asarnow, D.,Wang, Y.,Julius, D.,Cheng, Y.,van der Wijst, J. (deposition date: 2019-02-22, release date: 2019-04-24, Last modification date: 2024-03-20)

Primary citation

Dang, S.,van Goor, M.K.,Asarnow, D.,Wang, Y.,Julius, D.,Cheng, Y.,van der Wijst, J.
Structural insight into TRPV5 channel function and modulation.
Proc.Natl.Acad.Sci.USA, 116:8869-8878, 2019

PubMed Abstract: 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.

PubMed: 30975749
DOI: 10.1073/pnas.1820323116

Experimental method

ELECTRON MICROSCOPY (3.3 Å)