Identification and characterization of a large family of superbinding bacterial SH2 domains

SH2 domains bind to tyrosine-phosphorylated proteins and play crucial roles in signal transduction in mammalian cells. Here, Kaneko et al. identify a large family of SH2 domains in the bacterial pathogen Legionella that bind to mammalian phosphorylated proteins, in some cases with very high affinity...

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Autores principales:	Tomonori Kaneko, Peter J. Stogios, Xiang Ruan, Courtney Voss, Elena Evdokimova, Tatiana Skarina, Amy Chung, Xiaoling Liu, Lei Li, Alexei Savchenko, Alexander W. Ensminger, Shawn S.-C. Li
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/4802b25f8b354260bed6a583ba5257d2
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spelling	oai:doaj.org-article:4802b25f8b354260bed6a583ba5257d22021-12-02T14:40:31ZIdentification and characterization of a large family of superbinding bacterial SH2 domains10.1038/s41467-018-06943-22041-1723https://doaj.org/article/4802b25f8b354260bed6a583ba5257d22018-10-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-06943-2https://doaj.org/toc/2041-1723SH2 domains bind to tyrosine-phosphorylated proteins and play crucial roles in signal transduction in mammalian cells. Here, Kaneko et al. identify a large family of SH2 domains in the bacterial pathogen Legionella that bind to mammalian phosphorylated proteins, in some cases with very high affinity.Tomonori KanekoPeter J. StogiosXiang RuanCourtney VossElena EvdokimovaTatiana SkarinaAmy ChungXiaoling LiuLei LiAlexei SavchenkoAlexander W. EnsmingerShawn S.-C. LiNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-15 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Tomonori Kaneko Peter J. Stogios Xiang Ruan Courtney Voss Elena Evdokimova Tatiana Skarina Amy Chung Xiaoling Liu Lei Li Alexei Savchenko Alexander W. Ensminger Shawn S.-C. Li Identification and characterization of a large family of superbinding bacterial SH2 domains
description	SH2 domains bind to tyrosine-phosphorylated proteins and play crucial roles in signal transduction in mammalian cells. Here, Kaneko et al. identify a large family of SH2 domains in the bacterial pathogen Legionella that bind to mammalian phosphorylated proteins, in some cases with very high affinity.
format	article
author	Tomonori Kaneko Peter J. Stogios Xiang Ruan Courtney Voss Elena Evdokimova Tatiana Skarina Amy Chung Xiaoling Liu Lei Li Alexei Savchenko Alexander W. Ensminger Shawn S.-C. Li
author_facet	Tomonori Kaneko Peter J. Stogios Xiang Ruan Courtney Voss Elena Evdokimova Tatiana Skarina Amy Chung Xiaoling Liu Lei Li Alexei Savchenko Alexander W. Ensminger Shawn S.-C. Li
author_sort	Tomonori Kaneko
title	Identification and characterization of a large family of superbinding bacterial SH2 domains
title_short	Identification and characterization of a large family of superbinding bacterial SH2 domains
title_full	Identification and characterization of a large family of superbinding bacterial SH2 domains
title_fullStr	Identification and characterization of a large family of superbinding bacterial SH2 domains
title_full_unstemmed	Identification and characterization of a large family of superbinding bacterial SH2 domains
title_sort	identification and characterization of a large family of superbinding bacterial sh2 domains
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/4802b25f8b354260bed6a583ba5257d2
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Identification and characterization of a large family of superbinding bacterial SH2 domains

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