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
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Acceso en línea:https://doaj.org/article/031b403abc3941b8bfde584589cc3cd7
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Sumario: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.