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Conformational ensemble of the human TRPV3 ion channel

Author

Listed:
  • Lejla Zubcevic

    (Duke University Medical Center)

  • Mark A. Herzik

    (The Scripps Research Institute)

  • Mengyu Wu

    (The Scripps Research Institute
    The Scripps Research Institute)

  • William F. Borschel

    (Duke University Medical Center)

  • Marscha Hirschi

    (Duke University Medical Center
    The Scripps Research Institute)

  • Albert S. Song

    (The Scripps Research Institute
    The Scripps Research Institute)

  • Gabriel C. Lander

    (The Scripps Research Institute)

  • Seok-Yong Lee

    (Duke University Medical Center)

Abstract

Transient receptor potential vanilloid channel 3 (TRPV3), a member of the thermosensitive TRP (thermoTRPV) channels, is activated by warm temperatures and serves as a key regulator of normal skin physiology through the release of pro-inflammatory messengers. Mutations in trpv3 have been identified as the cause of the congenital skin disorder, Olmsted syndrome. Unlike other members of the thermoTRPV channel family, TRPV3 sensitizes upon repeated stimulation, yet a lack of structural information about the channel precludes a molecular-level understanding of TRPV3 sensitization and gating. Here, we present the cryo-electron microscopy structures of apo and sensitized human TRPV3, as well as several structures of TRPV3 in the presence of the common thermoTRPV agonist 2-aminoethoxydiphenyl borate (2-APB). Our results show α-to-π-helix transitions in the S6 during sensitization, and suggest a critical role for the S4-S5 linker π-helix during ligand-dependent gating.

Suggested Citation

  • Lejla Zubcevic & Mark A. Herzik & Mengyu Wu & William F. Borschel & Marscha Hirschi & Albert S. Song & Gabriel C. Lander & Seok-Yong Lee, 2018. "Conformational ensemble of the human TRPV3 ion channel," Nature Communications, Nature, vol. 9(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-07117-w
    DOI: 10.1038/s41467-018-07117-w
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    Cited by:

    1. Navid Paknejad & Vinay Sapuru & Richard K. Hite, 2023. "Structural titration reveals Ca2+-dependent conformational landscape of the IP3 receptor," Nature Communications, Nature, vol. 14(1), pages 1-20, December.
    2. 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.

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