Bromodomain
Bromodomains are a family of evolutionarily conserved protein modules of approximately 110 amino acids that have been found in chromatin-associated proteins as well as nuclear histone acetyltransferases (HATs). Besides its role in chromatin remodeling, recent studies have identified that bromodomains, as acetyl-lysine binding domains, are able to recognize and bind ε–N-acetylated lysine residues in histone and non-histone proteins. The nuclear magnetic resonance (NMR) spectroscopic analysis reveals that the chemical structure of bromodomains, consisting of four left-handed α-helices (including αZ, αA, αB and αC) connected by two loops (ZA and BC loops), forms a deep hydrophobic cavity serving as the acetyl-lysine recognition site.
- B5670 I-BET 151 hydrochloride1 CitationSummary: BET bromodomain inhibitor
- B4895 OF-1Summary: BRPF1B and BRPF2 bromodomain inhibitor
- B4915 BAZ2-ICRSummary: Selective BAZ2 bromodomain inhibitor
- B4916 GSK 5959Summary: BRPF1 bromodomain inhibitor
- B4917 Ischemin sodium saltSummary: CBP bromodomain inhibitor
- B4918 OXF BD 02Summary: Selective inhibitor of the first bromodomain of BRD4
- B5973 PFI 4Summary: Potent and selective BRPF1 Bromodomain inhibitor
- B5998 GSK2801Summary: inhibitor of BAZ2A and BAZ2B bromodomains
- B6169 I-BRD9Summary: BRD9 inhibitor
- B6184 BI-9564Summary: BRD9/7 specific inhibitor