Structural basis of temperature sensation by the TRP channel TRPV3

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 undergoe α-to-π transitions. Dur...

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Detalles Bibliográficos
Autores principales: Singh, Appu K., McGoldrick, Luke L., Demirkhanyan, Lusine, Leslie, Merfilius, Zakharian, Eleonora, Sobolevsky, Alexander I.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2019
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6858569/
https://www.ncbi.nlm.nih.gov/pubmed/31636415
http://dx.doi.org/10.1038/s41594-019-0318-7
Descripción
Sumario: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 undergoe 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 C-terminal and linker domains.

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