An allosteric conduit facilitates dynamic multisite substrate recognition by the SCFCdc4 ubiquitin ligase

The WD40 domain of the SCFCdc4ubiquitin ligase targets substrates via multiple phosphorylated degron motifs. The authors define a second degron-binding WD40 pocket that imparts a negative allosteric effect on binding to the primary pocket, and thereby enables the dynamic exchange of bound degrons.

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Autores principales:	Veronika Csizmok, Stephen Orlicky, Jing Cheng, Jianhui Song, Alaji Bah, Neda Delgoshaie, Hong Lin, Tanja Mittag, Frank Sicheri, Hue Sun Chan, Mike Tyers, Julie D. Forman-Kay
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/3ceb544c2e084e38929cafb11be01401
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spelling	oai:doaj.org-article:3ceb544c2e084e38929cafb11be014012021-12-02T14:42:16ZAn allosteric conduit facilitates dynamic multisite substrate recognition by the SCFCdc4 ubiquitin ligase10.1038/ncomms139432041-1723https://doaj.org/article/3ceb544c2e084e38929cafb11be014012017-01-01T00:00:00Zhttps://doi.org/10.1038/ncomms13943https://doaj.org/toc/2041-1723The WD40 domain of the SCFCdc4ubiquitin ligase targets substrates via multiple phosphorylated degron motifs. The authors define a second degron-binding WD40 pocket that imparts a negative allosteric effect on binding to the primary pocket, and thereby enables the dynamic exchange of bound degrons.Veronika CsizmokStephen OrlickyJing ChengJianhui SongAlaji BahNeda DelgoshaieHong LinTanja MittagFrank SicheriHue Sun ChanMike TyersJulie D. Forman-KayNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-14 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Veronika Csizmok Stephen Orlicky Jing Cheng Jianhui Song Alaji Bah Neda Delgoshaie Hong Lin Tanja Mittag Frank Sicheri Hue Sun Chan Mike Tyers Julie D. Forman-Kay An allosteric conduit facilitates dynamic multisite substrate recognition by the SCFCdc4 ubiquitin ligase
description	The WD40 domain of the SCFCdc4ubiquitin ligase targets substrates via multiple phosphorylated degron motifs. The authors define a second degron-binding WD40 pocket that imparts a negative allosteric effect on binding to the primary pocket, and thereby enables the dynamic exchange of bound degrons.
format	article
author	Veronika Csizmok Stephen Orlicky Jing Cheng Jianhui Song Alaji Bah Neda Delgoshaie Hong Lin Tanja Mittag Frank Sicheri Hue Sun Chan Mike Tyers Julie D. Forman-Kay
author_facet	Veronika Csizmok Stephen Orlicky Jing Cheng Jianhui Song Alaji Bah Neda Delgoshaie Hong Lin Tanja Mittag Frank Sicheri Hue Sun Chan Mike Tyers Julie D. Forman-Kay
author_sort	Veronika Csizmok
title	An allosteric conduit facilitates dynamic multisite substrate recognition by the SCFCdc4 ubiquitin ligase
title_short	An allosteric conduit facilitates dynamic multisite substrate recognition by the SCFCdc4 ubiquitin ligase
title_full	An allosteric conduit facilitates dynamic multisite substrate recognition by the SCFCdc4 ubiquitin ligase
title_fullStr	An allosteric conduit facilitates dynamic multisite substrate recognition by the SCFCdc4 ubiquitin ligase
title_full_unstemmed	An allosteric conduit facilitates dynamic multisite substrate recognition by the SCFCdc4 ubiquitin ligase
title_sort	allosteric conduit facilitates dynamic multisite substrate recognition by the scfcdc4 ubiquitin ligase
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/3ceb544c2e084e38929cafb11be01401
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An allosteric conduit facilitates dynamic multisite substrate recognition by the SCFCdc4 ubiquitin ligase

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