BRWD3 Inhibitors

BRWD3 inhibitors constitute a diverse class of chemicals that primarily target bromodomains and modify histone acetylation patterns, potentially influencing BRWD3's interactions and function. Bromodomain inhibitors, like JQ1 and I-BET151, specifically bind to the acetyl-lysine recognition pocket within bromodomains. This binding can impair BRWD3's ability to recognize and bind to acetylated lysines on histones or other proteins, a fundamental aspect of its protein-protein interaction modality.

Histone deacetylase inhibitors, such as VPA and SAHA, represent another segment of BRWD3 inhibitors. These compounds increase the overall acetylation levels of histones. Acetylated histones can serve as docking sites for proteins possessing bromodomains. Thus, an increase in histone acetylation might lead to a changed landscape of protein-protein interactions for BRWD3. On the other hand, compounds like GSK126 and UNC1999 inhibit the methyltransferase activity of enzymes like EZH2.