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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Main Authors:	Xiao Cong, Yang Liu, Wen Liu, Xiaowen Liang, Arthur Laganowsky
Format:	Article
Language:	English
Published:	Nature Publishing Group 2017-12-01
Series:	Nature Communications
Online Access:	https://doi.org/10.1038/s41467-017-02397-0

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spelling	doaj-dc1f3924235f40738b0ccffe352d66b12021-05-11T07:57:57ZengNature Publishing GroupNature Communications2041-17232017-12-01811810.1038/s41467-017-02397-0Allosteric modulation of protein-protein interactions by individual lipid binding eventsXiao Cong0Yang Liu1Wen Liu2Xiaowen Liang3Arthur Laganowsky4Institute of Biosciences and Technology, Texas A&M Health Science CenterInstitute of Biosciences and Technology, Texas A&M Health Science CenterInstitute of Biosciences and Technology, Texas A&M Health Science CenterInstitute of Biosciences and Technology, Texas A&M Health Science CenterInstitute of Biosciences and Technology, Texas A&M Health Science CenterNative 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.https://doi.org/10.1038/s41467-017-02397-0
collection	DOAJ
language	English
format	Article
sources	DOAJ
author	Xiao Cong Yang Liu Wen Liu Xiaowen Liang Arthur Laganowsky
spellingShingle	Xiao Cong Yang Liu Wen Liu Xiaowen Liang Arthur Laganowsky Allosteric modulation of protein-protein interactions by individual lipid binding events Nature Communications
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 Publishing Group
series	Nature Communications
issn	2041-1723
publishDate	2017-12-01
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.
url	https://doi.org/10.1038/s41467-017-02397-0
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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