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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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Detalles Bibliográficos
Autores principales: Toma-Fukai, Sachiko, Shimizu, Toshiyuki
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8586995/
https://www.ncbi.nlm.nih.gov/pubmed/34771091
http://dx.doi.org/10.3390/molecules26216682
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author Toma-Fukai, Sachiko
Shimizu, Toshiyuki
author_facet Toma-Fukai, Sachiko
Shimizu, Toshiyuki
author_sort Toma-Fukai, Sachiko
collection PubMed
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.
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spelling pubmed-85869952021-11-13 Structural Diversity of Ubiquitin E3 Ligase Toma-Fukai, Sachiko Shimizu, Toshiyuki Molecules Review 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. MDPI 2021-11-04 /pmc/articles/PMC8586995/ /pubmed/34771091 http://dx.doi.org/10.3390/molecules26216682 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Toma-Fukai, Sachiko
Shimizu, Toshiyuki
Structural Diversity of Ubiquitin E3 Ligase
title 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_short Structural Diversity of Ubiquitin E3 Ligase
title_sort structural diversity of ubiquitin e3 ligase
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8586995/
https://www.ncbi.nlm.nih.gov/pubmed/34771091
http://dx.doi.org/10.3390/molecules26216682
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