6O1P
Cryo-EM structure of full length TRPV5 in nanodisc
Summary for 6O1P
| Entry DOI | 10.2210/pdb6o1p/pdb |
| EMDB information | 0593 0594 |
| Descriptor | Transient receptor potential cation channel subfamily V member 5 (1 entity in total) |
| Functional Keywords | ion channel, trp channel, membrane protein |
| Biological source | Oryctolagus cuniculus (Rabbit) |
| Total number of polymer chains | 4 |
| Total formula weight | 331598.62 |
| Authors | Dang, S.,van Goor, M.K.,Asarnow, D.,Wang, Y.,Julius, D.,Cheng, Y.,van der Wijst, J. (deposition date: 2019-02-21, 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 Cited by 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: 30975749DOI: 10.1073/pnas.1820323116 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3 Å) |
Structure validation
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