Discovery of an exosite on the SOCS2-SH2 domain that enhances SH2 binding to phosphorylated ligands

SOCS2 is a key regulator of growth hormone and cytokine signaling, which recognizes phosphotyrosine (pTyr)-modified targets via a central SH2 domain. Here, the authors discover and characterize an exosite on this SH2 domain that can bind a non-phosphorylated peptide to enhance SOCS2:pTyr affinity.

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Autores principales:	Edmond M. Linossi, Kunlun Li, Gianluca Veggiani, Cyrus Tan, Farhad Dehkhoda, Colin Hockings, Dale J. Calleja, Narelle Keating, Rebecca Feltham, Andrew J. Brooks, Shawn S. Li, Sachdev S. Sidhu, Jeffrey J. Babon, Nadia J. Kershaw, Sandra E. Nicholson
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/c6fcc1c1f3344e70a63c5dfee1ef2786
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spelling	oai:doaj.org-article:c6fcc1c1f3344e70a63c5dfee1ef27862021-12-05T12:22:44ZDiscovery of an exosite on the SOCS2-SH2 domain that enhances SH2 binding to phosphorylated ligands10.1038/s41467-021-26983-52041-1723https://doaj.org/article/c6fcc1c1f3344e70a63c5dfee1ef27862021-12-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-26983-5https://doaj.org/toc/2041-1723SOCS2 is a key regulator of growth hormone and cytokine signaling, which recognizes phosphotyrosine (pTyr)-modified targets via a central SH2 domain. Here, the authors discover and characterize an exosite on this SH2 domain that can bind a non-phosphorylated peptide to enhance SOCS2:pTyr affinity.Edmond M. LinossiKunlun LiGianluca VeggianiCyrus TanFarhad DehkhodaColin HockingsDale J. CallejaNarelle KeatingRebecca FelthamAndrew J. BrooksShawn S. LiSachdev S. SidhuJeffrey J. BabonNadia J. KershawSandra E. NicholsonNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-13 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Edmond M. Linossi Kunlun Li Gianluca Veggiani Cyrus Tan Farhad Dehkhoda Colin Hockings Dale J. Calleja Narelle Keating Rebecca Feltham Andrew J. Brooks Shawn S. Li Sachdev S. Sidhu Jeffrey J. Babon Nadia J. Kershaw Sandra E. Nicholson Discovery of an exosite on the SOCS2-SH2 domain that enhances SH2 binding to phosphorylated ligands
description	SOCS2 is a key regulator of growth hormone and cytokine signaling, which recognizes phosphotyrosine (pTyr)-modified targets via a central SH2 domain. Here, the authors discover and characterize an exosite on this SH2 domain that can bind a non-phosphorylated peptide to enhance SOCS2:pTyr affinity.
format	article
author	Edmond M. Linossi Kunlun Li Gianluca Veggiani Cyrus Tan Farhad Dehkhoda Colin Hockings Dale J. Calleja Narelle Keating Rebecca Feltham Andrew J. Brooks Shawn S. Li Sachdev S. Sidhu Jeffrey J. Babon Nadia J. Kershaw Sandra E. Nicholson
author_facet	Edmond M. Linossi Kunlun Li Gianluca Veggiani Cyrus Tan Farhad Dehkhoda Colin Hockings Dale J. Calleja Narelle Keating Rebecca Feltham Andrew J. Brooks Shawn S. Li Sachdev S. Sidhu Jeffrey J. Babon Nadia J. Kershaw Sandra E. Nicholson
author_sort	Edmond M. Linossi
title	Discovery of an exosite on the SOCS2-SH2 domain that enhances SH2 binding to phosphorylated ligands
title_short	Discovery of an exosite on the SOCS2-SH2 domain that enhances SH2 binding to phosphorylated ligands
title_full	Discovery of an exosite on the SOCS2-SH2 domain that enhances SH2 binding to phosphorylated ligands
title_fullStr	Discovery of an exosite on the SOCS2-SH2 domain that enhances SH2 binding to phosphorylated ligands
title_full_unstemmed	Discovery of an exosite on the SOCS2-SH2 domain that enhances SH2 binding to phosphorylated ligands
title_sort	discovery of an exosite on the socs2-sh2 domain that enhances sh2 binding to phosphorylated ligands
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/c6fcc1c1f3344e70a63c5dfee1ef2786
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Discovery of an exosite on the SOCS2-SH2 domain that enhances SH2 binding to phosphorylated ligands

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