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Cryo-electron microscopy structure of the TRPV2 ion channel.

Publication ,  Journal Article
Zubcevic, L; Herzik, MA; Chung, BC; Liu, Z; Lander, GC; Lee, S-Y
Published in: Nat Struct Mol Biol
February 2016

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.

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Published In

Nat Struct Mol Biol

DOI

EISSN

1545-9985

Publication Date

February 2016

Volume

23

Issue

2

Start / End Page

180 / 186

Location

United States

Related Subject Headings

  • TRPV Cation Channels
  • Rabbits
  • Protein Conformation
  • Models, Molecular
  • Developmental Biology
  • Cryoelectron Microscopy
  • Biophysics
  • Ankyrin Repeat
  • Animals
  • 34 Chemical sciences
 

Citation

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Zubcevic, L., Herzik, M. A., Chung, B. C., Liu, Z., Lander, G. C., & Lee, S.-Y. (2016). Cryo-electron microscopy structure of the TRPV2 ion channel. Nat Struct Mol Biol, 23(2), 180–186. https://doi.org/10.1038/nsmb.3159
Zubcevic, Lejla, Mark A. Herzik, Ben C. Chung, Zhirui Liu, Gabriel C. Lander, and Seok-Yong Lee. “Cryo-electron microscopy structure of the TRPV2 ion channel.Nat Struct Mol Biol 23, no. 2 (February 2016): 180–86. https://doi.org/10.1038/nsmb.3159.
Zubcevic L, Herzik MA, Chung BC, Liu Z, Lander GC, Lee S-Y. Cryo-electron microscopy structure of the TRPV2 ion channel. Nat Struct Mol Biol. 2016 Feb;23(2):180–6.
Zubcevic, Lejla, et al. “Cryo-electron microscopy structure of the TRPV2 ion channel.Nat Struct Mol Biol, vol. 23, no. 2, Feb. 2016, pp. 180–86. Pubmed, doi:10.1038/nsmb.3159.
Zubcevic L, Herzik MA, Chung BC, Liu Z, Lander GC, Lee S-Y. Cryo-electron microscopy structure of the TRPV2 ion channel. Nat Struct Mol Biol. 2016 Feb;23(2):180–186.

Published In

Nat Struct Mol Biol

DOI

EISSN

1545-9985

Publication Date

February 2016

Volume

23

Issue

2

Start / End Page

180 / 186

Location

United States

Related Subject Headings

  • TRPV Cation Channels
  • Rabbits
  • Protein Conformation
  • Models, Molecular
  • Developmental Biology
  • Cryoelectron Microscopy
  • Biophysics
  • Ankyrin Repeat
  • Animals
  • 34 Chemical sciences