Conformational ensemble of the human TRPV3 ion channel

Lejla Zubcevic, Mark A. Herzik, Mengyu Wu, William F. Borschel, Marscha Hirschi, Albert S. Song, Gabriel C. Lander () and Seok-Yong Lee ()
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Lejla Zubcevic: Duke University Medical Center
Mark A. Herzik: The Scripps Research Institute
Mengyu Wu: The Scripps Research Institute
William F. Borschel: Duke University Medical Center
Marscha Hirschi: Duke University Medical Center
Albert S. Song: The Scripps Research Institute
Gabriel C. Lander: The Scripps Research Institute
Seok-Yong Lee: Duke University Medical Center

Nature Communications, 2018, vol. 9, issue 1, 1-12

Abstract: 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.

Date: 2018
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DOI: 10.1038/s41467-018-07117-w

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