Structural Diversity of Ubiquitin E3 Ligase

The post-translational modification of proteins regulates many biological processes. Their dysfunction relates to diseases. Ubiquitination is one of the post-translational modifications that target lysine residue and regulate many cellular processes. Three enzymes are required for achieving the ubiq...

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Autores principales:	Sachiko Toma-Fukai, Toshiyuki Shimizu
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	post-translational modification ubiquitin E3 ligase structural biology X-ray crystallography Organic chemistry QD241-441
Acceso en línea:	https://doaj.org/article/7b645b9f48f54a99abbfda8e54e7b102
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spelling	oai:doaj.org-article:7b645b9f48f54a99abbfda8e54e7b1022021-11-11T18:38:21ZStructural Diversity of Ubiquitin E3 Ligase10.3390/molecules262166821420-3049https://doaj.org/article/7b645b9f48f54a99abbfda8e54e7b1022021-11-01T00:00:00Zhttps://www.mdpi.com/1420-3049/26/21/6682https://doaj.org/toc/1420-3049The post-translational modification of proteins regulates many biological processes. Their dysfunction relates to diseases. Ubiquitination is one of the post-translational modifications that target lysine residue and regulate many cellular processes. Three enzymes are required for achieving the ubiquitination reaction: ubiquitin-activating enzyme (E1), ubiquitin-conjugating enzyme (E2), and ubiquitin ligase (E3). E3s play a pivotal role in selecting substrates. Many structural studies have been conducted to reveal the molecular mechanism of the ubiquitination reaction. Recently, the structure of PCAF_N, a newly categorized E3 ligase, was reported. We present a review of the recent progress toward the structural understanding of E3 ligases.Sachiko Toma-FukaiToshiyuki ShimizuMDPI AGarticlepost-translational modificationubiquitin E3 ligasestructural biologyX-ray crystallographyOrganic chemistryQD241-441ENMolecules, Vol 26, Iss 6682, p 6682 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	post-translational modification ubiquitin E3 ligase structural biology X-ray crystallography Organic chemistry QD241-441
spellingShingle	post-translational modification ubiquitin E3 ligase structural biology X-ray crystallography Organic chemistry QD241-441 Sachiko Toma-Fukai Toshiyuki Shimizu Structural Diversity of Ubiquitin E3 Ligase
description	The post-translational modification of proteins regulates many biological processes. Their dysfunction relates to diseases. Ubiquitination is one of the post-translational modifications that target lysine residue and regulate many cellular processes. Three enzymes are required for achieving the ubiquitination reaction: ubiquitin-activating enzyme (E1), ubiquitin-conjugating enzyme (E2), and ubiquitin ligase (E3). E3s play a pivotal role in selecting substrates. Many structural studies have been conducted to reveal the molecular mechanism of the ubiquitination reaction. Recently, the structure of PCAF_N, a newly categorized E3 ligase, was reported. We present a review of the recent progress toward the structural understanding of E3 ligases.
format	article
author	Sachiko Toma-Fukai Toshiyuki Shimizu
author_facet	Sachiko Toma-Fukai Toshiyuki Shimizu
author_sort	Sachiko Toma-Fukai
title	Structural Diversity of Ubiquitin E3 Ligase
title_short	Structural Diversity of Ubiquitin E3 Ligase
title_full	Structural Diversity of Ubiquitin E3 Ligase
title_fullStr	Structural Diversity of Ubiquitin E3 Ligase
title_full_unstemmed	Structural Diversity of Ubiquitin E3 Ligase
title_sort	structural diversity of ubiquitin e3 ligase
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/7b645b9f48f54a99abbfda8e54e7b102
work_keys_str_mv	AT sachikotomafukai structuraldiversityofubiquitine3ligase AT toshiyukishimizu structuraldiversityofubiquitine3ligase
_version_	1718431771265073152

Structural Diversity of Ubiquitin E3 Ligase

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