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Structure of the full-length TRPV2 channel by cryo-EM

Author

Listed:
  • Kevin W. Huynh

    (School of Medicine, Case Western Reserve University, 10900 Euclid Avenue, Wood Building, W151D, Cleveland, Ohio 44106, USA)

  • Matthew R. Cohen

    (School of Medicine, Case Western Reserve University, 10900 Euclid Avenue, Wood Building, W151D, Cleveland, Ohio 44106, USA
    School of Medicine, Case Western Reserve University)

  • Jiansen Jiang

    (Immunology and Molecular Genetics, University of California
    California NanoSystems Institute, University of California)

  • Amrita Samanta

    (School of Medicine, Case Western Reserve University, 10900 Euclid Avenue, Wood Building, W151D, Cleveland, Ohio 44106, USA
    School of Medicine, Case Western Reserve University)

  • David T. Lodowski

    (School of Medicine, Case Western Reserve University, 10900 Euclid Avenue, Wood Building, W151D, Cleveland, Ohio 44106, USA
    School of Medicine, Case Western Reserve University)

  • Z. Hong Zhou

    (Immunology and Molecular Genetics, University of California
    California NanoSystems Institute, University of California)

  • Vera Y. Moiseenkova-Bell

    (School of Medicine, Case Western Reserve University, 10900 Euclid Avenue, Wood Building, W151D, Cleveland, Ohio 44106, USA
    School of Medicine, Case Western Reserve University)

Abstract

Transient receptor potential (TRP) proteins form a superfamily Ca2+-permeable cation channels regulated by a range of chemical and physical stimuli. Structural analysis of a ‘minimal’ TRP vanilloid subtype 1 (TRPV1) elucidated a mechanism of channel activation by agonists through changes in its outer pore region. Though homologous to TRPV1, other TRPV channels (TRPV2–6) are insensitive to TRPV1 activators including heat and vanilloids. To further understand the structural basis of TRPV channel function, we determined the structure of full-length TRPV2 at ∼5 Å resolution by cryo-electron microscopy. Like TRPV1, TRPV2 contains two constrictions, one each in the pore-forming upper and lower gates. The agonist-free full-length TRPV2 has wider upper and lower gates compared with closed and agonist-activated TRPV1. We propose these newly revealed TRPV2 structural features contribute to diversity of TRPV channels.

Suggested Citation

  • Kevin W. Huynh & Matthew R. Cohen & Jiansen Jiang & Amrita Samanta & David T. Lodowski & Z. Hong Zhou & Vera Y. Moiseenkova-Bell, 2016. "Structure of the full-length TRPV2 channel by cryo-EM," Nature Communications, Nature, vol. 7(1), pages 1-8, September.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms11130
    DOI: 10.1038/ncomms11130
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    Cited by:

    1. Ruth A. Pumroy & Anna D. Protopopova & Tabea C. Fricke & Iris U. Lange & Ferdinand M. Haug & Phuong T. Nguyen & Pamela N. Gallo & Bárbara B. Sousa & Gonçalo J. L. Bernardes & Vladimir Yarov-Yarovoy & , 2022. "Structural insights into TRPV2 activation by small molecules," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
    2. Liying Zhang & Charlotte Simonsen & Lucie Zimova & Kaituo Wang & Lavanya Moparthi & Rachelle Gaudet & Maria Ekoff & Gunnar Nilsson & Ute A. Hellmich & Viktorie Vlachova & Pontus Gourdon & Peter M. Zyg, 2022. "Cannabinoid non-cannabidiol site modulation of TRPV2 structure and function," Nature Communications, Nature, vol. 13(1), pages 1-18, December.

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