Structural Diversity of Ubiquitin E3 Ligase
Copyright policy )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 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.
Models, Molecular, Protein Conformation, Ubiquitin-Protein Ligases, Amino Acid Motifs, Organic chemistry, Review, Crystallography, X-Ray, ubiquitin E3 ligase, Structure-Activity Relationship, QD241-441, structural biology, Humans, Protein Isoforms, Protein Interaction Domains and Motifs, Amino Acid Sequence, X-ray crystallography, Ubiquitin, Ubiquitination, post-translational modification, Multigene Family, Ubiquitin-Conjugating Enzymes, Protein Processing, Post-Translational, Protein Binding
Models, Molecular, Protein Conformation, Ubiquitin-Protein Ligases, Amino Acid Motifs, Organic chemistry, Review, Crystallography, X-Ray, ubiquitin E3 ligase, Structure-Activity Relationship, QD241-441, structural biology, Humans, Protein Isoforms, Protein Interaction Domains and Motifs, Amino Acid Sequence, X-ray crystallography, Ubiquitin, Ubiquitination, post-translational modification, Multigene Family, Ubiquitin-Conjugating Enzymes, Protein Processing, Post-Translational, Protein Binding
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