@article{bibcite_468,
  keywords = {Crystallography, X-Ray, Humans, Molecular Docking Simulation, Binding Sites, Ligands, Molecular Structure, Water, Nuclear Proteins, Protein Interaction Domains and Motifs, Protein Domains, Adaptor Proteins, Signal Transducing},
  author = {J. Zhu and A. Caflisch},
  title = {Twenty crystal structures of bromodomain and PHD finger containing protein 1 (BRPF1)/ligand complexes reveal conserved binding motifs and rare interactions},
  abstract = {<p>BRPF1 plays a scaffolding role in transcription. We report on fragment screening by high-throughput docking to the BRPF1 bromodomain which resulted in six chemotypes with very favorable ligand efficiency (0.45-0.50 kcal/mol per non-hydrogen atom). Twenty crystal structures of BRPF1/ligand complexes show structural conservation in the acetyllysine binding site, common binding motifs, and unusual interactions (e.g., the replacement of a conserved water molecule). The structural information is useful for the design of chemical probes.</p>},
  year = {2016},
  journal = {Journal of Medicinal Chemistry},
  volume = {59},
  chapter = {5555},
  pages = {5555-5561},
  month = {2016 Jun 09},
  issn = {1520-4804},
  doi = {10.1021/acs.jmedchem.6b00215},
  language = {eng},
}