Cryo-EM structures of the TTYH family reveal a novel architecture for lipid interactions

The human Tweety homologue (TTYH) family of transmembrane proteins have been suggested to act as chloride channels. Here the authors present cryo-EM structures of the 3 human TTYH paralogs that do not display the expected features of an anion channel, and instead appear to interact with lipid-like c...

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Autores principales: Anastasiia Sukalskaia, Monique S. Straub, Dawid Deneka, Marta Sawicka, Raimund Dutzler
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2021
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Acceso en línea:https://doaj.org/article/2d2881505759441e904cbd1e682b44ed
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spelling oai:doaj.org-article:2d2881505759441e904cbd1e682b44ed2021-12-02T15:07:48ZCryo-EM structures of the TTYH family reveal a novel architecture for lipid interactions10.1038/s41467-021-25106-42041-1723https://doaj.org/article/2d2881505759441e904cbd1e682b44ed2021-08-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-25106-4https://doaj.org/toc/2041-1723The human Tweety homologue (TTYH) family of transmembrane proteins have been suggested to act as chloride channels. Here the authors present cryo-EM structures of the 3 human TTYH paralogs that do not display the expected features of an anion channel, and instead appear to interact with lipid-like compounds residing in the membrane; suggesting an involvement in lipid-associated processes.Anastasiia SukalskaiaMonique S. StraubDawid DenekaMarta SawickaRaimund DutzlerNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Anastasiia Sukalskaia
Monique S. Straub
Dawid Deneka
Marta Sawicka
Raimund Dutzler
Cryo-EM structures of the TTYH family reveal a novel architecture for lipid interactions
description The human Tweety homologue (TTYH) family of transmembrane proteins have been suggested to act as chloride channels. Here the authors present cryo-EM structures of the 3 human TTYH paralogs that do not display the expected features of an anion channel, and instead appear to interact with lipid-like compounds residing in the membrane; suggesting an involvement in lipid-associated processes.
format article
author Anastasiia Sukalskaia
Monique S. Straub
Dawid Deneka
Marta Sawicka
Raimund Dutzler
author_facet Anastasiia Sukalskaia
Monique S. Straub
Dawid Deneka
Marta Sawicka
Raimund Dutzler
author_sort Anastasiia Sukalskaia
title Cryo-EM structures of the TTYH family reveal a novel architecture for lipid interactions
title_short Cryo-EM structures of the TTYH family reveal a novel architecture for lipid interactions
title_full Cryo-EM structures of the TTYH family reveal a novel architecture for lipid interactions
title_fullStr Cryo-EM structures of the TTYH family reveal a novel architecture for lipid interactions
title_full_unstemmed Cryo-EM structures of the TTYH family reveal a novel architecture for lipid interactions
title_sort cryo-em structures of the ttyh family reveal a novel architecture for lipid interactions
publisher Nature Portfolio
publishDate 2021
url https://doaj.org/article/2d2881505759441e904cbd1e682b44ed
work_keys_str_mv AT anastasiiasukalskaia cryoemstructuresofthettyhfamilyrevealanovelarchitectureforlipidinteractions
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AT dawiddeneka cryoemstructuresofthettyhfamilyrevealanovelarchitectureforlipidinteractions
AT martasawicka cryoemstructuresofthettyhfamilyrevealanovelarchitectureforlipidinteractions
AT raimunddutzler cryoemstructuresofthettyhfamilyrevealanovelarchitectureforlipidinteractions
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