@article{bibcite_467,
  keywords = {Computer Simulation, Crystallography, X-Ray, Humans, Molecular Docking Simulation, Binding Sites, Ligands, Proteins, Nuclear Proteins, Protein Structure, Tertiary, Indoles, Small Molecule Libraries, Lysine, CREB-Binding Protein, Adaptor Proteins, Signal Transducing, Chemistry Techniques, Synthetic, Indolizines},
  author = {A. Unzue and H. Zhao and G. Lolli and J. Dong and J. Zhu and M. Zechner and A. Dolbois and A. Caflisch and C. Nevado},
  title = {The "gatekeeper" residue influences the mode of binding of acetyl indoles to bromodomains},
  abstract = {<p>Small-molecule hits for the bromodomains of CREBBP and BAZ2B have been identified by scaffold hopping followed by docking of a set of \~{}200 compounds containing the acetyl indole scaffold. Chemical synthesis of nearly 30 derivatives has resulted in ligands of representatives of three subfamilies of human bromodomains with favorable ligand efficiency. The X-ray crystal structures of three different bromodomains (CREBBP, BAZ2B, and BRPF1b) in complex with acetyl indole derivatives reveal the influence of the gatekeeper residue on the orientation of small-molecule ligands in the acetyl lysine binding site.</p>},
  year = {2016},
  journal = {Journal of Medicinal Chemistry},
  volume = {59},
  chapter = {3087},
  pages = {3087-3097},
  month = {2016 Apr 14},
  issn = {1520-4804},
  doi = {10.1021/acs.jmedchem.5b01757},
  language = {eng},
}