A dual role for the N-terminal domain of the IL-3 receptor in cell signalling

The N-terminal domain (NTD) of interleukin-3 receptor α-subunit (IL3Rα) is involved in IL-3 recognition but the underlying mechanism is unknown. Here, the authors present crystal structures of the IL3Rα complex and provide biochemical evidence that the NTD regulates IL-3 binding and signalling compl...

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Autores principales:	Sophie E. Broughton, Timothy R. Hercus, Tracy L. Nero, Winnie L. Kan, Emma F. Barry, Mara Dottore, Karen S. Cheung Tung Shing, Craig J. Morton, Urmi Dhagat, Matthew P. Hardy, Nicholas J. Wilson, Matthew T. Downton, Christine Schieber, Timothy P. Hughes, Angel F. Lopez, Michael W. Parker
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/a177e8976263487282e8d1895527256b
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spelling	oai:doaj.org-article:a177e8976263487282e8d1895527256b2021-12-02T15:34:46ZA dual role for the N-terminal domain of the IL-3 receptor in cell signalling10.1038/s41467-017-02633-72041-1723https://doaj.org/article/a177e8976263487282e8d1895527256b2018-01-01T00:00:00Zhttps://doi.org/10.1038/s41467-017-02633-7https://doaj.org/toc/2041-1723The N-terminal domain (NTD) of interleukin-3 receptor α-subunit (IL3Rα) is involved in IL-3 recognition but the underlying mechanism is unknown. Here, the authors present crystal structures of the IL3Rα complex and provide biochemical evidence that the NTD regulates IL-3 binding and signalling complex assembly.Sophie E. BroughtonTimothy R. HercusTracy L. NeroWinnie L. KanEmma F. BarryMara DottoreKaren S. Cheung Tung ShingCraig J. MortonUrmi DhagatMatthew P. HardyNicholas J. WilsonMatthew T. DowntonChristine SchieberTimothy P. HughesAngel F. LopezMichael W. ParkerNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-15 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Sophie E. Broughton Timothy R. Hercus Tracy L. Nero Winnie L. Kan Emma F. Barry Mara Dottore Karen S. Cheung Tung Shing Craig J. Morton Urmi Dhagat Matthew P. Hardy Nicholas J. Wilson Matthew T. Downton Christine Schieber Timothy P. Hughes Angel F. Lopez Michael W. Parker A dual role for the N-terminal domain of the IL-3 receptor in cell signalling
description	The N-terminal domain (NTD) of interleukin-3 receptor α-subunit (IL3Rα) is involved in IL-3 recognition but the underlying mechanism is unknown. Here, the authors present crystal structures of the IL3Rα complex and provide biochemical evidence that the NTD regulates IL-3 binding and signalling complex assembly.
format	article
author	Sophie E. Broughton Timothy R. Hercus Tracy L. Nero Winnie L. Kan Emma F. Barry Mara Dottore Karen S. Cheung Tung Shing Craig J. Morton Urmi Dhagat Matthew P. Hardy Nicholas J. Wilson Matthew T. Downton Christine Schieber Timothy P. Hughes Angel F. Lopez Michael W. Parker
author_facet	Sophie E. Broughton Timothy R. Hercus Tracy L. Nero Winnie L. Kan Emma F. Barry Mara Dottore Karen S. Cheung Tung Shing Craig J. Morton Urmi Dhagat Matthew P. Hardy Nicholas J. Wilson Matthew T. Downton Christine Schieber Timothy P. Hughes Angel F. Lopez Michael W. Parker
author_sort	Sophie E. Broughton
title	A dual role for the N-terminal domain of the IL-3 receptor in cell signalling
title_short	A dual role for the N-terminal domain of the IL-3 receptor in cell signalling
title_full	A dual role for the N-terminal domain of the IL-3 receptor in cell signalling
title_fullStr	A dual role for the N-terminal domain of the IL-3 receptor in cell signalling
title_full_unstemmed	A dual role for the N-terminal domain of the IL-3 receptor in cell signalling
title_sort	dual role for the n-terminal domain of the il-3 receptor in cell signalling
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/a177e8976263487282e8d1895527256b
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A dual role for the N-terminal domain of the IL-3 receptor in cell signalling

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