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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Auteurs principaux:	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
Format:	article
Langue:	EN
Publié:	Nature Portfolio 2017
Sujets:	Science Q
Accès en ligne:	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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_version_	1718381606945685504

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

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