Bromodomain-containing proteins are a group of proteins that play a crucial role in regulating gene expression by recognizing and binding to acetylated lysine residues on histone and non-histone proteins. Among these, Bromodomain Containing 2 (BRD2) is a significant member of the BET (Bromodomain and Extra-Terminal domain) family, which also includes BRD3, BRD4, and BRDT .
BRD2 contains two tandem bromodomains (BD1 and BD2) at its N-terminus and a conserved ET (Extra-Terminal) domain at its C-terminus . These bromodomains are structurally conserved epigenetic reader domains that bind to acetylated lysine residues, facilitating the regulation of gene expression . The two bromodomains of BRD2 have distinct roles:
BRD2 is involved in various biological processes, including cell cycle regulation, transcriptional activation, and chromatin remodeling . It acts as a scaffold protein, assembling multi-protein complexes that regulate diverse biological pathways . The interaction of BRD2 with acetylated histones is crucial for the regulation of gene expression, particularly during cell division and differentiation .
Research on BRD2 has provided insights into its role in various diseases, including cancer and inflammatory disorders. The development of small molecule inhibitors targeting BRD2 and other BET proteins has shown promise in preclinical studies for treating these conditions . Human recombinant BRD2 is used in research to study its structure, function, and interactions with other proteins, aiding in the development of therapeutic strategies.