Structural basis for chemokine receptor CCR6 activation by the endogenous protein ligand CCL20

Chemokine receptors are GPCRs involved in immune responses and regulated by small protein ligands known as chemokines. A structural study of the human CCR6/CCL20–Go complex reveals that CCL20 binds in a shallow extracellular pocket, and suggests that activation of CCR6 by CCL20 binding involves an a...

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Autores principales:	David Jonathan Wasilko, Zachary Lee Johnson, Mark Ammirati, Ye Che, Matthew C. Griffor, Seungil Han, Huixian Wu
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/563862bc1d384d9c84f3cca32e285ede
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spelling	oai:doaj.org-article:563862bc1d384d9c84f3cca32e285ede2021-12-02T16:04:25ZStructural basis for chemokine receptor CCR6 activation by the endogenous protein ligand CCL2010.1038/s41467-020-16820-62041-1723https://doaj.org/article/563862bc1d384d9c84f3cca32e285ede2020-06-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-16820-6https://doaj.org/toc/2041-1723Chemokine receptors are GPCRs involved in immune responses and regulated by small protein ligands known as chemokines. A structural study of the human CCR6/CCL20–Go complex reveals that CCL20 binds in a shallow extracellular pocket, and suggests that activation of CCR6 by CCL20 binding involves an allosteric effect on a noncanonical toggle switch.David Jonathan WasilkoZachary Lee JohnsonMark AmmiratiYe CheMatthew C. GrifforSeungil HanHuixian WuNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-9 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q David Jonathan Wasilko Zachary Lee Johnson Mark Ammirati Ye Che Matthew C. Griffor Seungil Han Huixian Wu Structural basis for chemokine receptor CCR6 activation by the endogenous protein ligand CCL20
description	Chemokine receptors are GPCRs involved in immune responses and regulated by small protein ligands known as chemokines. A structural study of the human CCR6/CCL20–Go complex reveals that CCL20 binds in a shallow extracellular pocket, and suggests that activation of CCR6 by CCL20 binding involves an allosteric effect on a noncanonical toggle switch.
format	article
author	David Jonathan Wasilko Zachary Lee Johnson Mark Ammirati Ye Che Matthew C. Griffor Seungil Han Huixian Wu
author_facet	David Jonathan Wasilko Zachary Lee Johnson Mark Ammirati Ye Che Matthew C. Griffor Seungil Han Huixian Wu
author_sort	David Jonathan Wasilko
title	Structural basis for chemokine receptor CCR6 activation by the endogenous protein ligand CCL20
title_short	Structural basis for chemokine receptor CCR6 activation by the endogenous protein ligand CCL20
title_full	Structural basis for chemokine receptor CCR6 activation by the endogenous protein ligand CCL20
title_fullStr	Structural basis for chemokine receptor CCR6 activation by the endogenous protein ligand CCL20
title_full_unstemmed	Structural basis for chemokine receptor CCR6 activation by the endogenous protein ligand CCL20
title_sort	structural basis for chemokine receptor ccr6 activation by the endogenous protein ligand ccl20
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/563862bc1d384d9c84f3cca32e285ede
work_keys_str_mv	AT davidjonathanwasilko structuralbasisforchemokinereceptorccr6activationbytheendogenousproteinligandccl20 AT zacharyleejohnson structuralbasisforchemokinereceptorccr6activationbytheendogenousproteinligandccl20 AT markammirati structuralbasisforchemokinereceptorccr6activationbytheendogenousproteinligandccl20 AT yeche structuralbasisforchemokinereceptorccr6activationbytheendogenousproteinligandccl20 AT matthewcgriffor structuralbasisforchemokinereceptorccr6activationbytheendogenousproteinligandccl20 AT seungilhan structuralbasisforchemokinereceptorccr6activationbytheendogenousproteinligandccl20 AT huixianwu structuralbasisforchemokinereceptorccr6activationbytheendogenousproteinligandccl20
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Structural basis for chemokine receptor CCR6 activation by the endogenous protein ligand CCL20

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