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. Author manuscript; available in PMC: 2011 Jun 23.
Published in final edited form as: Nature. 2010 Sep 24;468(7327):1067–1073. doi: 10.1038/nature09504

Figure 2. Characterization of BET complexes with (+)-JQ1.

Figure 2

a, Superimposition of the mouse BRD4(1)/H3K14ac peptide complex28 with the human BRD4(1)/(+)-JQ1 complex structure. The hydrogen bond formed to the conserved asparagine (N140) in the peptide complex is shown as yellow dots. b, 2Fo-Fc map of (+)-JQ1 in complex with BRD4(1) contoured at 2σ. c, Electrostatic surface of BRD4(1) in complex with (+)-JQ1. The ligand is shown as a CPK model demonstrating the excellent shape complimentarity with the protein acetylated lysine receptor site. d, Ribbon diagram of the complex of human BRD4(1) with (+)-JQ1 in CPK representation. The main secondary structural elements and the conserved active site asparagine side chain (N140) are labelled.