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.
- A4184 PFI-1 (PF-6405761)1 CitationTarget: BromodomainsSummary: BET inhibitor
- A4186 Bromosporine1 CitationTarget: BromodomainsSummary: Bromodomain inhibitor,non-selective
- A1910 Bromodomain Inhibitor, (+)-JQ138 CitationTarget: BromodomainsSummary: BET bromodomain inhibitor
- A3445 GSK 525768ASummary: inactive stereoisomer of I-BET-762
- A3692 OTX-0153 CitationTarget: BromodomainsSummary: BRD inhibitor
- A3901 UNC12151 CitationTarget: L3MBTLSummary: Chemical probe for the methyllysine (Kme)
- B6169 I-BRD9Summary: BRD9 inhibitor
- B6184 BI-9564Summary: BRD9/7 specific inhibitor
- B6196 BI-7273Summary: BRD9 bromodomain inhibitor
- B6197 PF-CBP1 hydrochlorideSummary: CBP/p300 bromodomain inhibitor