Structure of bromodomain and its interactions

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A bromodomain is a protein domain that recognizes acetylated lysine residues on a histone in post-translational modifications. In certain species, hyperacetylation becomes evident during spermiogenesis, just before chromatin compaction begins. Bromodomains typically consist of two asymmetrical domains, but the 3D model depicted here is of a single bromodomain (BD1), which is represented in all white, bound to an acetylated histone protein – H4K5acK8ac peptide. The yellow compound corresponds to the histone protein bound to BD1. Also highlighted on BD1 are specific side chains that play a crucial role in binding to the histone protein. References: Morinière, J., Rousseaux, S., Steuerwald, U. et al. Cooperative binding of two acetylation marks on a histone tail by a single bromodomain. Nature 461, 664–668 (2009). https://doi.org/10.1038/nature08397