Structure of the full-length TRPV2 channel by cryo-EM

Transient receptor potential (TRP) proteins are Ca2+-permeable cation channels activated by a range of chemical and physical stimuli. Here the authors describe a cryo-EM structure of the full-length TRPV2 channel that provides insight into the regulation of the TRPV subfamily of channels.

Guardado en:
Detalles Bibliográficos
Autores principales: Kevin W. Huynh, Matthew R. Cohen, Jiansen Jiang, Amrita Samanta, David T. Lodowski, Z. Hong Zhou, Vera Y. Moiseenkova-Bell
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2016
Materias:
Q
Acceso en línea:https://doaj.org/article/70c38fe2d52a4df989a42f15648a4e47
Etiquetas: Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
id oai:doaj.org-article:70c38fe2d52a4df989a42f15648a4e47
record_format dspace
spelling oai:doaj.org-article:70c38fe2d52a4df989a42f15648a4e472021-12-02T15:35:23ZStructure of the full-length TRPV2 channel by cryo-EM10.1038/ncomms111302041-1723https://doaj.org/article/70c38fe2d52a4df989a42f15648a4e472016-03-01T00:00:00Zhttps://doi.org/10.1038/ncomms11130https://doaj.org/toc/2041-1723Transient receptor potential (TRP) proteins are Ca2+-permeable cation channels activated by a range of chemical and physical stimuli. Here the authors describe a cryo-EM structure of the full-length TRPV2 channel that provides insight into the regulation of the TRPV subfamily of channels.Kevin W. HuynhMatthew R. CohenJiansen JiangAmrita SamantaDavid T. LodowskiZ. Hong ZhouVera Y. Moiseenkova-BellNature PortfolioarticleScienceQENNature Communications, Vol 7, Iss 1, Pp 1-8 (2016)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Kevin W. Huynh
Matthew R. Cohen
Jiansen Jiang
Amrita Samanta
David T. Lodowski
Z. Hong Zhou
Vera Y. Moiseenkova-Bell
Structure of the full-length TRPV2 channel by cryo-EM
description Transient receptor potential (TRP) proteins are Ca2+-permeable cation channels activated by a range of chemical and physical stimuli. Here the authors describe a cryo-EM structure of the full-length TRPV2 channel that provides insight into the regulation of the TRPV subfamily of channels.
format article
author Kevin W. Huynh
Matthew R. Cohen
Jiansen Jiang
Amrita Samanta
David T. Lodowski
Z. Hong Zhou
Vera Y. Moiseenkova-Bell
author_facet Kevin W. Huynh
Matthew R. Cohen
Jiansen Jiang
Amrita Samanta
David T. Lodowski
Z. Hong Zhou
Vera Y. Moiseenkova-Bell
author_sort Kevin W. Huynh
title Structure of the full-length TRPV2 channel by cryo-EM
title_short 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_sort structure of the full-length trpv2 channel by cryo-em
publisher Nature Portfolio
publishDate 2016
url https://doaj.org/article/70c38fe2d52a4df989a42f15648a4e47
work_keys_str_mv AT kevinwhuynh structureofthefulllengthtrpv2channelbycryoem
AT matthewrcohen structureofthefulllengthtrpv2channelbycryoem
AT jiansenjiang structureofthefulllengthtrpv2channelbycryoem
AT amritasamanta structureofthefulllengthtrpv2channelbycryoem
AT davidtlodowski structureofthefulllengthtrpv2channelbycryoem
AT zhongzhou structureofthefulllengthtrpv2channelbycryoem
AT veraymoiseenkovabell structureofthefulllengthtrpv2channelbycryoem
_version_ 1718386602915397632