Evidence that the TRPV1 S1-S4 membrane domain contributes to thermosensing

The TRPV1 ion channel is a heat-sensing receptor that is also activated by vanilloid compounds, but the molecular underpinnings of thermosensing have remained elusive. Here authors use in solution NMR on the isolated human TRPV1 S1-S4 domain and show that this domain undergoes a non-denaturing tempe...

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Autores principales:	Minjoo Kim, Nicholas J. Sisco, Jacob K. Hilton, Camila M. Montano, Manuel A. Castro, Brian R. Cherry, Marcia Levitus, Wade D. Van Horn
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/031b403abc3941b8bfde584589cc3cd7
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spelling	oai:doaj.org-article:031b403abc3941b8bfde584589cc3cd72021-12-02T15:10:40ZEvidence that the TRPV1 S1-S4 membrane domain contributes to thermosensing10.1038/s41467-020-18026-22041-1723https://doaj.org/article/031b403abc3941b8bfde584589cc3cd72020-08-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-18026-2https://doaj.org/toc/2041-1723The TRPV1 ion channel is a heat-sensing receptor that is also activated by vanilloid compounds, but the molecular underpinnings of thermosensing have remained elusive. Here authors use in solution NMR on the isolated human TRPV1 S1-S4 domain and show that this domain undergoes a non-denaturing temperature-dependent transition with a high thermosensitivity.Minjoo KimNicholas J. SiscoJacob K. HiltonCamila M. MontanoManuel A. CastroBrian R. CherryMarcia LevitusWade D. Van HornNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-16 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Minjoo Kim Nicholas J. Sisco Jacob K. Hilton Camila M. Montano Manuel A. Castro Brian R. Cherry Marcia Levitus Wade D. Van Horn Evidence that the TRPV1 S1-S4 membrane domain contributes to thermosensing
description	The TRPV1 ion channel is a heat-sensing receptor that is also activated by vanilloid compounds, but the molecular underpinnings of thermosensing have remained elusive. Here authors use in solution NMR on the isolated human TRPV1 S1-S4 domain and show that this domain undergoes a non-denaturing temperature-dependent transition with a high thermosensitivity.
format	article
author	Minjoo Kim Nicholas J. Sisco Jacob K. Hilton Camila M. Montano Manuel A. Castro Brian R. Cherry Marcia Levitus Wade D. Van Horn
author_facet	Minjoo Kim Nicholas J. Sisco Jacob K. Hilton Camila M. Montano Manuel A. Castro Brian R. Cherry Marcia Levitus Wade D. Van Horn
author_sort	Minjoo Kim
title	Evidence that the TRPV1 S1-S4 membrane domain contributes to thermosensing
title_short	Evidence that the TRPV1 S1-S4 membrane domain contributes to thermosensing
title_full	Evidence that the TRPV1 S1-S4 membrane domain contributes to thermosensing
title_fullStr	Evidence that the TRPV1 S1-S4 membrane domain contributes to thermosensing
title_full_unstemmed	Evidence that the TRPV1 S1-S4 membrane domain contributes to thermosensing
title_sort	evidence that the trpv1 s1-s4 membrane domain contributes to thermosensing
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/031b403abc3941b8bfde584589cc3cd7
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Evidence that the TRPV1 S1-S4 membrane domain contributes to thermosensing

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