Bromodomain adjacent to zinc finger domain protein 2B (BAZ2B) (BAZ2B)

Bromodomain adjacent to zinc finger domain protein 2B (BAZ2B) is a critical epigenetic reader protein that plays a significant role in chromatin remodeling and the regulation of gene expression. It contains a C-terminal bromodomain that specifically recognizes and binds to acetylated lysine residues on histone tails, such as H3K14ac, thereby recruiting transcriptional machinery to specific genomic loci [UniProt: Q9UIF8]. BAZ2B has been identified as a potential therapeutic target due to its involvement in the maintenance and differentiation of hematopoietic stem cells and its association with various diseases, including leukemia and certain neurological disorders [PubMed: 25605333]. Small-molecule inhibitors, such as GSK2820151 and BAZ2-ICR, have been developed as chemical probes to selectively target the BAZ2B bromodomain, disrupting its interaction with chromatin and modulating downstream gene expression [PubMed: 26151304]. These pharmacological tools are essential for validating BAZ2B as a drug target and understanding its complex role in human physiology and pathology [PubMed: 24654318].

Other names

BAZ2-BWALp4hWALp4Transcription termination factor I-interacting protein 4

Competitive inhibition of the bromodomain acetyl-lysine binding pocket, preventing the recognition of acetylated lysine residues on histones and subsequent recruitment of chromatin-remodeling complexes.