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Nat Struct Mol Biol. 2016 Feb;23(2):180-6. doi: 10.1038/nsmb.3159. Epub 2016 Jan 18.

Cryo-electron microscopy structure of the TRPV2 ion channel.

Author information

1
Department of Biochemistry, Duke University Medical Center, Durham, North Carolina, USA.
2
Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California, USA.

Abstract

Transient receptor potential vanilloid (TRPV) cation channels are polymodal sensors involved in a variety of physiological processes. TRPV2, a member of the TRPV family, is regulated by temperature, by ligands, such as probenecid and cannabinoids, and by lipids. TRPV2 has been implicated in many biological functions, including somatosensation, osmosensation and innate immunity. Here we present the atomic model of rabbit TRPV2 in its putative desensitized state, as determined by cryo-EM at a nominal resolution of ∼4 Å. In the TRPV2 structure, the transmembrane segment 6 (S6), which is involved in gate opening, adopts a conformation different from the one observed in TRPV1. Structural comparisons of TRPV1 and TRPV2 indicate that a rotation of the ankyrin-repeat domain is coupled to pore opening via the TRP domain, and this pore opening can be modulated by rearrangements in the secondary structure of S6.

PMID:
26779611
PMCID:
PMC4876856
DOI:
10.1038/nsmb.3159
[Indexed for MEDLINE]
Free PMC Article
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