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Structural basis of temperature sensation by the TRP channel TRPV3.

ABSTRACT: We present structures of mouse TRPV3 in temperature-dependent open, closed and intermediate states that suggest two-step activation of TRPV3 by heat. During the strongly temperature-dependent first step, sensitization, the channel pore remains closed while S6 helices undergo ?-to-? transitions. During the weakly temperature-dependent second step, channel opening, tight association of the S1-S4 and pore domains is stabilized by changes in the carboxy-terminal and linker domains.

SUBMITTER: Singh AK

PROVIDER: S-EPMC6858569 | biostudies-literature | 2019 Nov

REPOSITORIES: biostudies-literature

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Structural basis of temperature sensation by the TRP channel TRPV3.

Singh Appu K AK McGoldrick Luke L LL Demirkhanyan Lusine L Leslie Merfilius M Zakharian Eleonora E Sobolevsky Alexander I AI

Nature structural & molecular biology 20191021 11

We present structures of mouse TRPV3 in temperature-dependent open, closed and intermediate states that suggest two-step activation of TRPV3 by heat. During the strongly temperature-dependent first step, sensitization, the channel pore remains closed while S6 helices undergo α-to-π transitions. During the weakly temperature-dependent second step, channel opening, tight association of the S1-S4 and pore domains is stabilized by changes in the carboxy-terminal and linker domains. ...[more]

PMID: 31636415

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