CREB-binding protein (CBP) has a bromodomain that recognises the acetylation of the lysine residue at position 56 on histone 3. CBP recognises and anchors to histone 3 by a couple different mechanisms illustrated in this model. They involve interactions between CBP’s hydrophobic ligand binding site and a key amino acids on the H3 peptide. How CBP identifies H3K56ac is crucial as CBP also posesses a histone acetyltransferase domain, which allows acetylation of free histones.
Xu, L., Cheng, A., Huang, M., Zhang, J., Jiang, Y., Wang, C., Li, F., Bao, H., Gao, J., Wang, N. and Liu, J., 2017. Structural insight into the recognition of acetylated histone H3K56ac mediated by the bromodomain of CREB‐binding protein. The FEBS journal, 284(20), pp.3422-3436.
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