What you see here is chain A & P of the mouse Brdt protein, a testis-specific member of the Bromodomains and extraterminal (BET) protein family, that’s a homologue of the human TAF1 protein. The Brdt protein recognises and binds to di(or more)-acetylated H3 and H4 histone tails to form part of an enzyme complex that performs chromatin remodelling (the displacement or reorganisation of nucleosomes) for upregulation of expression of particular genes following hyperacetylation during spermiogenesis.
In particular, the BD1 bromodomain (on chain A) of Brdt forms high-affinity interactions with acetylated Lysine 5 and 8 residues on histone H4 tails (H4K5acK8ac). This guided tour delves into the BD1 bromodomain binding pocket and the key structural features contained within, the types of interactions they form and mutations that change the ability for ligand recognition. This protein, model 2wp2, is from the PDB and information comes from the associated paper (DOI: 10.1038/nature08397)
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