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...
| Main Authors: | , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2021-11-01
|
| Series: | Molecules |
| Subjects: | |
| Online Access: | https://www.mdpi.com/1420-3049/26/21/6682 |
| _version_ | 1797512008464072704 |
|---|---|
| author | Sachiko Toma-Fukai Toshiyuki Shimizu |
| author_facet | Sachiko Toma-Fukai Toshiyuki Shimizu |
| author_sort | Sachiko Toma-Fukai |
| collection | DOAJ |
| 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. |
| first_indexed | 2024-03-10T05:54:55Z |
| format | Article |
| id | doaj.art-7b645b9f48f54a99abbfda8e54e7b102 |
| institution | Directory Open Access Journal |
| issn | 1420-3049 |
| language | English |
| last_indexed | 2024-03-10T05:54:55Z |
| publishDate | 2021-11-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Molecules |
| spelling | doaj.art-7b645b9f48f54a99abbfda8e54e7b1022023-11-22T21:25:00ZengMDPI AGMolecules1420-30492021-11-012621668210.3390/molecules26216682Structural Diversity of Ubiquitin E3 LigaseSachiko Toma-Fukai0Toshiyuki Shimizu1Graduate School of Science and Technology, Nara Institute of Science and Technology, 8916-5 Takayama-cho, Ikoma 630-0192, JapanGraduate School of Pharmaceutical Sciences, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, JapanThe 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.https://www.mdpi.com/1420-3049/26/21/6682post-translational modificationubiquitin E3 ligasestructural biologyX-ray crystallography |
| spellingShingle | Sachiko Toma-Fukai Toshiyuki Shimizu Structural Diversity of Ubiquitin E3 Ligase Molecules post-translational modification ubiquitin E3 ligase structural biology X-ray crystallography |
| 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 | post-translational modification ubiquitin E3 ligase structural biology X-ray crystallography |
| url | https://www.mdpi.com/1420-3049/26/21/6682 |
| work_keys_str_mv | AT sachikotomafukai structuraldiversityofubiquitine3ligase AT toshiyukishimizu structuraldiversityofubiquitine3ligase |