Abstract
The bromodomain is a structurally conserved protein module that is present in a large number of chromatin-associated proteins and in many nuclear histone acetyltransferases. The bromodomain functions as an acetyl-lysine binding domain and has recently been shown to play an important role in regulating protein-protein interactions in chromatin-mediated cellular gene transcription as well as in viral transcriptional activation. Recent structural analyses of bromodomains in complex with acetyl-lysine-containing biological ligands provide insights into the molecular basis of differences in ligand selectivity of the bromodomain family, and reinforce the concept that functional diversity of a conserved protein structure is achieved by evolutionary changes of amino acid sequences in the ligand binding site.
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Yan, K.S., Zhou, MM. (2005). The Structure and Molecular Interactions of the Bromodomain. In: Waksman, G. (eds) Proteomics and Protein-Protein Interactions. Protein Reviews, vol 3. Springer, Boston, MA. https://doi.org/10.1007/0-387-24532-4_10
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