Allosteric modulation of protein-protein interactions by individual lipid binding events

Native mass spectrometry (MS) is a technique that preserves non-covalent interactions in the mass spectrometer. Here the authors use native MS to study integral membrane proteins, and find that lipids with different headgroups and tails can allosterically modulate protein-protein interactions in dif...

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Autores principales:	Xiao Cong, Yang Liu, Wen Liu, Xiaowen Liang, Arthur Laganowsky
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/dc1f3924235f40738b0ccffe352d66b1
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spelling	oai:doaj.org-article:dc1f3924235f40738b0ccffe352d66b12021-12-02T15:37:07ZAllosteric modulation of protein-protein interactions by individual lipid binding events10.1038/s41467-017-02397-02041-1723https://doaj.org/article/dc1f3924235f40738b0ccffe352d66b12017-12-01T00:00:00Zhttps://doi.org/10.1038/s41467-017-02397-0https://doaj.org/toc/2041-1723Native mass spectrometry (MS) is a technique that preserves non-covalent interactions in the mass spectrometer. Here the authors use native MS to study integral membrane proteins, and find that lipids with different headgroups and tails can allosterically modulate protein-protein interactions in different fashions.Xiao CongYang LiuWen LiuXiaowen LiangArthur LaganowskyNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-8 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Xiao Cong Yang Liu Wen Liu Xiaowen Liang Arthur Laganowsky Allosteric modulation of protein-protein interactions by individual lipid binding events
description	Native mass spectrometry (MS) is a technique that preserves non-covalent interactions in the mass spectrometer. Here the authors use native MS to study integral membrane proteins, and find that lipids with different headgroups and tails can allosterically modulate protein-protein interactions in different fashions.
format	article
author	Xiao Cong Yang Liu Wen Liu Xiaowen Liang Arthur Laganowsky
author_facet	Xiao Cong Yang Liu Wen Liu Xiaowen Liang Arthur Laganowsky
author_sort	Xiao Cong
title	Allosteric modulation of protein-protein interactions by individual lipid binding events
title_short	Allosteric modulation of protein-protein interactions by individual lipid binding events
title_full	Allosteric modulation of protein-protein interactions by individual lipid binding events
title_fullStr	Allosteric modulation of protein-protein interactions by individual lipid binding events
title_full_unstemmed	Allosteric modulation of protein-protein interactions by individual lipid binding events
title_sort	allosteric modulation of protein-protein interactions by individual lipid binding events
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/dc1f3924235f40738b0ccffe352d66b1
work_keys_str_mv	AT xiaocong allostericmodulationofproteinproteininteractionsbyindividuallipidbindingevents AT yangliu allostericmodulationofproteinproteininteractionsbyindividuallipidbindingevents AT wenliu allostericmodulationofproteinproteininteractionsbyindividuallipidbindingevents AT xiaowenliang allostericmodulationofproteinproteininteractionsbyindividuallipidbindingevents AT arthurlaganowsky allostericmodulationofproteinproteininteractionsbyindividuallipidbindingevents
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Allosteric modulation of protein-protein interactions by individual lipid binding events

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