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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...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
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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. |
format | Online Article Text |
id | pubmed-8586995 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT tomafukaisachiko structuraldiversityofubiquitine3ligase AT shimizutoshiyuki structuraldiversityofubiquitine3ligase |