Structure of SgK223 pseudokinase reveals novel mechanisms of homotypic and heterotypic association

Pseudokinases lack kinase activity, yet they impact cellular physiology through the regulation of bona fide signaling kinases. Here the authors describe the structure of the SgK223 pseudokinase and its adjacent domains, and identify regulatory interfaces required for self-assembly and downstream sig...

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Autores principales: Onisha Patel, Michael D. W. Griffin, Santosh Panjikar, Weiwen Dai, Xiuquan Ma, Howard Chan, Celine Zheng, Ashleigh Kropp, James M. Murphy, Roger J. Daly, Isabelle S. Lucet
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Lenguaje:EN
Publicado: Nature Portfolio 2017
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Acceso en línea:https://doaj.org/article/3c3bd4fad8f44ebaa6db0fe88d4e53a6
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spelling oai:doaj.org-article:3c3bd4fad8f44ebaa6db0fe88d4e53a62021-12-02T17:06:28ZStructure of SgK223 pseudokinase reveals novel mechanisms of homotypic and heterotypic association10.1038/s41467-017-01279-92041-1723https://doaj.org/article/3c3bd4fad8f44ebaa6db0fe88d4e53a62017-10-01T00:00:00Zhttps://doi.org/10.1038/s41467-017-01279-9https://doaj.org/toc/2041-1723Pseudokinases lack kinase activity, yet they impact cellular physiology through the regulation of bona fide signaling kinases. Here the authors describe the structure of the SgK223 pseudokinase and its adjacent domains, and identify regulatory interfaces required for self-assembly and downstream signaling.Onisha PatelMichael D. W. GriffinSantosh PanjikarWeiwen DaiXiuquan MaHoward ChanCeline ZhengAshleigh KroppJames M. MurphyRoger J. DalyIsabelle S. LucetNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-15 (2017)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Onisha Patel
Michael D. W. Griffin
Santosh Panjikar
Weiwen Dai
Xiuquan Ma
Howard Chan
Celine Zheng
Ashleigh Kropp
James M. Murphy
Roger J. Daly
Isabelle S. Lucet
Structure of SgK223 pseudokinase reveals novel mechanisms of homotypic and heterotypic association
description Pseudokinases lack kinase activity, yet they impact cellular physiology through the regulation of bona fide signaling kinases. Here the authors describe the structure of the SgK223 pseudokinase and its adjacent domains, and identify regulatory interfaces required for self-assembly and downstream signaling.
format article
author Onisha Patel
Michael D. W. Griffin
Santosh Panjikar
Weiwen Dai
Xiuquan Ma
Howard Chan
Celine Zheng
Ashleigh Kropp
James M. Murphy
Roger J. Daly
Isabelle S. Lucet
author_facet Onisha Patel
Michael D. W. Griffin
Santosh Panjikar
Weiwen Dai
Xiuquan Ma
Howard Chan
Celine Zheng
Ashleigh Kropp
James M. Murphy
Roger J. Daly
Isabelle S. Lucet
author_sort Onisha Patel
title Structure of SgK223 pseudokinase reveals novel mechanisms of homotypic and heterotypic association
title_short Structure of SgK223 pseudokinase reveals novel mechanisms of homotypic and heterotypic association
title_full Structure of SgK223 pseudokinase reveals novel mechanisms of homotypic and heterotypic association
title_fullStr Structure of SgK223 pseudokinase reveals novel mechanisms of homotypic and heterotypic association
title_full_unstemmed Structure of SgK223 pseudokinase reveals novel mechanisms of homotypic and heterotypic association
title_sort structure of sgk223 pseudokinase reveals novel mechanisms of homotypic and heterotypic association
publisher Nature Portfolio
publishDate 2017
url https://doaj.org/article/3c3bd4fad8f44ebaa6db0fe88d4e53a6
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