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. 2015 Dec 8;13(12):e1002316. doi: 10.1371/journal.pbio.1002316

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© 2015 Schulz et al

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

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Fig 7 — (A) Structure of the Bdf2 bromodomain in complex with I-BET151 (PDB code 4PKL). (B) Electron density of I-BET151 and key residues for ligand recognition. The two conserved residues mutated to alanine in the Bdf2 mutant are colored in orange. (C) Superimposition of Bdf2 (cyan) in complex with I-BET151 (yellow) onto human BRD4-BD1 (light red, 3ZYU) in complex with I-BET151 (magenta). (D to F) Electrostatic surface potential shown between -10 kT/e (red) and +10kT/e (blue) of (D) trypanosome Bdf2 bromodomain in complex with I-BET151, (E) human BRD4-BD1 in complex with I-BET151 (3ZYU), and (F) human BRD9 in complex with a triazolophtalazine inhibitor (4NQN).