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TitleStructural insight into TRPV5 channel function and modulation.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 116, Issue 18, Page 8869-8878, Year 2019
Publish dateApr 30, 2019
AuthorsShangyu Dang / Mark K van Goor / Daniel Asarnow / YongQiang Wang / David Julius / Yifan Cheng / Jenny van der Wijst /
PubMed AbstractTRPV5 (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 linksProc Natl Acad Sci U S A / PubMed:30975749 / PubMed Central
MethodsEM (single particle)
Resolution2.8 - 3.3 Å
Structure data

0593

6o1n

EMDB-0593, PDB-6o1n:
Cryo-EM structure of TRPV5 (1-660) in nanodisc
Method: EM (single particle) / Resolution: 2.9 Å

0594

6o1p

EMDB-0594, PDB-6o1p:
Cryo-EM structure of full length TRPV5 in nanodisc
Method: EM (single particle) / Resolution: 3.0 Å

0605

6o1u

EMDB-0605, PDB-6o1u:
Cryo-EM structure of TRPV5 W583A in nanodisc
Method: EM (single particle) / Resolution: 2.8 Å

0607

6o20

EMDB-0607, PDB-6o20:
Cryo-EM structure of TRPV5 with calmodulin bound
Method: EM (single particle) / Resolution: 3.3 Å

Chemicals

ChemComp-CA:
Unknown entry

Source
  • oryctolagus cuniculus (rabbit)
  • bos taurus (cattle)
KeywordsMEMBRANE PROTEIN / ion channel / TRP channel

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