BET family bromodomain 2 (BET BD2)

The BET family bromodomains, specifically the second bromodomain (BD2), are evolutionarily conserved domains found in BRD2, BRD3, BRD4, and BRDT proteins. BD2 specifically recognizes acetylated lysine residues on histone tails, particularly H3 and H4, acting as an epigenetic “reader” and mediating chromatin remodeling and transcription regulation through recruitment of transcription factors and coactivators[1][2][4][5]. The two bromodomains (BD1 and BD2) prefer binding to di-acetylated lysines in histone marks, but they contribute independently to regulating gene expression and chromatin targeting[2][4][5]. BD2 has been structurally characterized and plays a crucial role in mitotic retention of BET proteins on chromosomes and in cell cycle progression[1][4]. Small-molecule inhibitors targeting BD2, especially those with BD2 selectivity, are under active investigation for cancer, inflammation, and other diseases due to their differential effects on gene expression and disease phenotypes[2][3][5].

Other names

second BET bromodomainBET protein BD2BRD4 bromodomain 2BRD2 bromodomain 2BET BDIIsecond bromodomain of BRD2/BRD3/BRD4/BRDT

Inhibition of bromodomain binding to acetylated lysines, displacing BET proteins from chromatin Disruption of transcriptional activation by preventing recruitment of transcription factors/coactivators to chromatin Suppression of oncogene (e.g., MYC) expression by interfering with super-enhancer function