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-Structure paper
Title | Structural insight into TRPV5 channel function and modulation. |
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Journal, issue, pages | Proc Natl Acad Sci U S A, Vol. 116, Issue 18, Page 8869-8878, Year 2019 |
Publish date | Apr 30, 2019 |
Authors | Shangyu Dang / Mark K van Goor / Daniel Asarnow / YongQiang Wang / David Julius / Yifan Cheng / Jenny van der Wijst / |
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 ...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. |
External links | Proc Natl Acad Sci U S A / PubMed:30975749 / PubMed Central |
Methods | EM (single particle) |
Resolution | 2.8 - 3.3 Å |
Structure data | EMDB-0593, PDB-6o1n: EMDB-0594, PDB-6o1p: |
Chemicals | ChemComp-CA: |
Source |
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Keywords | MEMBRANE PROTEIN / ion channel / TRP channel |