Structure and dynamics of the ASB9 CUL-RING E3 Ligase

Multi-subunit Cullin (CUL)-RING ligases (CRL) form the largest family of E3 ligases and are composed of a substrate receptor, a CUL, and a RING-box (RBX) protein. Here, the authors use cryo-EM and HDX-MS to characterise the ASB9 CUL-RING E3 ligase and present the structure of ASB9-ELOB/C bound to th...

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Autores principales:	Ryan J. Lumpkin, Richard W. Baker, Andres E. Leschziner, Elizabeth A. Komives
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/0bbb6cb9e2c74688aa91f0f7c786a41f
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spelling	oai:doaj.org-article:0bbb6cb9e2c74688aa91f0f7c786a41f2021-12-02T15:02:50ZStructure and dynamics of the ASB9 CUL-RING E3 Ligase10.1038/s41467-020-16499-92041-1723https://doaj.org/article/0bbb6cb9e2c74688aa91f0f7c786a41f2020-06-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-16499-9https://doaj.org/toc/2041-1723Multi-subunit Cullin (CUL)-RING ligases (CRL) form the largest family of E3 ligases and are composed of a substrate receptor, a CUL, and a RING-box (RBX) protein. Here, the authors use cryo-EM and HDX-MS to characterise the ASB9 CUL-RING E3 ligase and present the structure of ASB9-ELOB/C bound to the substrate creatine kinase and the full-length CUL5 structure in complex with RBX2, and they propose a revised allosteric mechanism for CUL-E3 ligase function.Ryan J. LumpkinRichard W. BakerAndres E. LeschzinerElizabeth A. KomivesNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-11 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Ryan J. Lumpkin Richard W. Baker Andres E. Leschziner Elizabeth A. Komives Structure and dynamics of the ASB9 CUL-RING E3 Ligase
description	Multi-subunit Cullin (CUL)-RING ligases (CRL) form the largest family of E3 ligases and are composed of a substrate receptor, a CUL, and a RING-box (RBX) protein. Here, the authors use cryo-EM and HDX-MS to characterise the ASB9 CUL-RING E3 ligase and present the structure of ASB9-ELOB/C bound to the substrate creatine kinase and the full-length CUL5 structure in complex with RBX2, and they propose a revised allosteric mechanism for CUL-E3 ligase function.
format	article
author	Ryan J. Lumpkin Richard W. Baker Andres E. Leschziner Elizabeth A. Komives
author_facet	Ryan J. Lumpkin Richard W. Baker Andres E. Leschziner Elizabeth A. Komives
author_sort	Ryan J. Lumpkin
title	Structure and dynamics of the ASB9 CUL-RING E3 Ligase
title_short	Structure and dynamics of the ASB9 CUL-RING E3 Ligase
title_full	Structure and dynamics of the ASB9 CUL-RING E3 Ligase
title_fullStr	Structure and dynamics of the ASB9 CUL-RING E3 Ligase
title_full_unstemmed	Structure and dynamics of the ASB9 CUL-RING E3 Ligase
title_sort	structure and dynamics of the asb9 cul-ring e3 ligase
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/0bbb6cb9e2c74688aa91f0f7c786a41f
work_keys_str_mv	AT ryanjlumpkin structureanddynamicsoftheasb9culringe3ligase AT richardwbaker structureanddynamicsoftheasb9culringe3ligase AT andreseleschziner structureanddynamicsoftheasb9culringe3ligase AT elizabethakomives structureanddynamicsoftheasb9culringe3ligase
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Structure and dynamics of the ASB9 CUL-RING E3 Ligase

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