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Structure of the full-length TRPV2 channel by cryo-EM
Transient receptor potential (TRP) proteins form a superfamily Ca(2+)-permeable cation channels regulated by a range of chemical and physical stimuli. Structural analysis of a ‘minimal' TRP vanilloid subtype 1 (TRPV1) elucidated a mechanism of channel activation by agonists through changes in i...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4820614/ https://www.ncbi.nlm.nih.gov/pubmed/27021073 http://dx.doi.org/10.1038/ncomms11130 |
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author | Huynh, Kevin W. Cohen, Matthew R. Jiang, Jiansen Samanta, Amrita Lodowski, David T. Zhou, Z. Hong Moiseenkova-Bell, Vera Y. |
author_facet | Huynh, Kevin W. Cohen, Matthew R. Jiang, Jiansen Samanta, Amrita Lodowski, David T. Zhou, Z. Hong Moiseenkova-Bell, Vera Y. |
author_sort | Huynh, Kevin W. |
collection | PubMed |
description | Transient receptor potential (TRP) proteins form a superfamily Ca(2+)-permeable cation channels regulated by a range of chemical and physical stimuli. Structural analysis of a ‘minimal' TRP vanilloid subtype 1 (TRPV1) elucidated a mechanism of channel activation by agonists through changes in its outer pore region. Though homologous to TRPV1, other TRPV channels (TRPV2–6) are insensitive to TRPV1 activators including heat and vanilloids. To further understand the structural basis of TRPV channel function, we determined the structure of full-length TRPV2 at ∼5 Å resolution by cryo-electron microscopy. Like TRPV1, TRPV2 contains two constrictions, one each in the pore-forming upper and lower gates. The agonist-free full-length TRPV2 has wider upper and lower gates compared with closed and agonist-activated TRPV1. We propose these newly revealed TRPV2 structural features contribute to diversity of TRPV channels. |
format | Online Article Text |
id | pubmed-4820614 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-48206142016-04-17 Structure of the full-length TRPV2 channel by cryo-EM Huynh, Kevin W. Cohen, Matthew R. Jiang, Jiansen Samanta, Amrita Lodowski, David T. Zhou, Z. Hong Moiseenkova-Bell, Vera Y. Nat Commun Article Transient receptor potential (TRP) proteins form a superfamily Ca(2+)-permeable cation channels regulated by a range of chemical and physical stimuli. Structural analysis of a ‘minimal' TRP vanilloid subtype 1 (TRPV1) elucidated a mechanism of channel activation by agonists through changes in its outer pore region. Though homologous to TRPV1, other TRPV channels (TRPV2–6) are insensitive to TRPV1 activators including heat and vanilloids. To further understand the structural basis of TRPV channel function, we determined the structure of full-length TRPV2 at ∼5 Å resolution by cryo-electron microscopy. Like TRPV1, TRPV2 contains two constrictions, one each in the pore-forming upper and lower gates. The agonist-free full-length TRPV2 has wider upper and lower gates compared with closed and agonist-activated TRPV1. We propose these newly revealed TRPV2 structural features contribute to diversity of TRPV channels. Nature Publishing Group 2016-03-29 /pmc/articles/PMC4820614/ /pubmed/27021073 http://dx.doi.org/10.1038/ncomms11130 Text en Copyright © 2016, Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved. http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article's Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ |
spellingShingle | Article Huynh, Kevin W. Cohen, Matthew R. Jiang, Jiansen Samanta, Amrita Lodowski, David T. Zhou, Z. Hong Moiseenkova-Bell, Vera Y. Structure of the full-length TRPV2 channel by cryo-EM |
title | Structure of the full-length TRPV2 channel by cryo-EM |
title_full | Structure of the full-length TRPV2 channel by cryo-EM |
title_fullStr | Structure of the full-length TRPV2 channel by cryo-EM |
title_full_unstemmed | Structure of the full-length TRPV2 channel by cryo-EM |
title_short | Structure of the full-length TRPV2 channel by cryo-EM |
title_sort | structure of the full-length trpv2 channel by cryo-em |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4820614/ https://www.ncbi.nlm.nih.gov/pubmed/27021073 http://dx.doi.org/10.1038/ncomms11130 |
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