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
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author Singh, Appu K.
McGoldrick, Luke L.
Demirkhanyan, Lusine
Leslie, Merfilius
Zakharian, Eleonora
Sobolevsky, Alexander I.
author_facet Singh, Appu K.
McGoldrick, Luke L.
Demirkhanyan, Lusine
Leslie, Merfilius
Zakharian, Eleonora
Sobolevsky, Alexander I.
author_sort Singh, Appu K.
collection PubMed
description 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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spelling pubmed-68585692020-04-21 Structural basis of temperature sensation by the TRP channel TRPV3 Singh, Appu K. McGoldrick, Luke L. Demirkhanyan, Lusine Leslie, Merfilius Zakharian, Eleonora Sobolevsky, Alexander I. Nat Struct Mol Biol Article 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. 2019-10-21 2019-11 /pmc/articles/PMC6858569/ /pubmed/31636415 http://dx.doi.org/10.1038/s41594-019-0318-7 Text en Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use:http://www.nature.com/authors/editorial_policies/license.html#terms Reprints and permissions information are available at www.nature.com/reprints (http://www.nature.com/reprints) .
spellingShingle Article
Singh, Appu K.
McGoldrick, Luke L.
Demirkhanyan, Lusine
Leslie, Merfilius
Zakharian, Eleonora
Sobolevsky, Alexander I.
Structural basis of temperature sensation by the TRP channel TRPV3
title Structural basis of temperature sensation by the TRP channel TRPV3
title_full Structural basis of temperature sensation by the TRP channel TRPV3
title_fullStr Structural basis of temperature sensation by the TRP channel TRPV3
title_full_unstemmed Structural basis of temperature sensation by the TRP channel TRPV3
title_short Structural basis of temperature sensation by the TRP channel TRPV3
title_sort structural basis of temperature sensation by the trp channel trpv3
topic Article
url 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
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