@article{bibcite_296,
  keywords = {Hydrogen Bonding, Protein Structure, Secondary, Protein Binding, Binding Sites, DNA-Binding Proteins, Nuclear Proteins, Protein Processing, Post-Translational, Protein Interaction Domains and Motifs, Chromosomal Proteins, Non-Histone, Histones, Molecular Dynamics Simulation, Acetylation, Adenosine Triphosphatases, Amino Acid Motifs, CREB-Binding Protein, DNA Helicases, Histone Acetyltransferases, TATA-Binding Protein Associated Factors, Transcription Factor TFIID, Transcription Factors},
  author = {S. Steiner and A. Magno and D. Huang and A. Caflisch},
  title = {Does bromodomain flexibility influence histone recognition?},
  abstract = {<p>Bromodomains are protein modules that selectively recognize histones by binding to acetylated lysines. Here, we have carried out multiple molecular dynamics simulations of 20 human bromodomains to investigate the flexibility of their binding site. Some bromodomains show alternative side chain orientations of three evolutionarily conserved residues: the Asn involved in acetyl-lysine binding and two conserved aromatic residues. Furthermore, for the BAZ2B and CREBBP bromodomains we observe occlusion of the binding site which is coupled to the displacement of the two aromatic residues. In contrast to available structures, the simulations reveal large variability of the binding site accessibility. The simulations suggest that the flexibility of the bromodomain binding site and presence of self-occluded metastable states influence the recognition of acetyl-lysine on histone tails.</p>},
  year = {2013},
  journal = {FEBS Letters},
  volume = {587},
  pages = {2158-2163},
  month = {2013 Jul 11},
  issn = {1873-3468},
  doi = {10.1016/j.febslet.2013.05.032},
  language = {eng},
}