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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Veröffentlicht in: | Molecules (Basel, Switzerland) Switzerland), 2021-11, Vol.26 (21), p.6682 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | 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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ISSN: | 1420-3049 1420-3049 |
DOI: | 10.3390/molecules26216682 |