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.
- C4229 UMB-32Summary: inhibitor of the BET bromodomain BRD4 and the bromodomain-containing transcription factor TAF1 and TAF1L
- C4097 NI-57Summary: bromodomains of BRPF proteins inhibitor
- C3668 GSK6853Summary: BRPF1 inhibitor
- C3076 AZD 5153Summary: orally available, bivalent inhibitor of the bromodomain and extraterminal (BET) protein BRD4.
- B7801 CPI-637Summary: CBP/EP300 bromodomain inhibitor
- B6197 PF-CBP1 hydrochlorideSummary: CBP/p300 bromodomain inhibitor
- B6196 BI-7273Summary: BRD9 bromodomain inhibitor
- B6184 BI-9564Summary: BRD9/7 specific inhibitor
- B6169 I-BRD9Summary: BRD9 inhibitor
- B5998 GSK2801Summary: inhibitor of BAZ2A and BAZ2B bromodomains