This review from Manfred Jung and colleagues looks at the structural biology and inhibition of bromodomains, enzymatic domains which recognise acetylated lysines residues in modified histones in chromatin. Inhibiting the protein–protein interactions in bromodomains by using small molecules as epigenetic tools is an exciting new area of research, offering potential for new therapeutic approaches.
The review includes:
- Structural features of bromodomains and acetyl-lysine recognition
- Implication of bromodomains in pathological cellular states
- Challenges by targeting protein–protein interactions with small molecules
- Inhibitors of bromodomain-mediated protein–protein interactions
- Inhibitors of the PCAF-BRD/HIV-TatK50ac interaction
- Inhibitors of the CBP-BRD/p53K382ac interaction
- Inhibitors of BET bromodomains
This hot review is part of our forthcoming themed issue on Epigenetics – keep checking back for more hot research in this theme:
Inhibition of bromodomain-mediated protein–protein interactions as a novel therapeutic strategy
Silviya D. Furdas, Luca Carlino, Wolfgang Sippl and Manfred Jung
DOI: 10.1039/C1MD00201E
