Structural implications for K5/K12-di-acetylated histone H4 recognition by the second bromodomain of BRD2.

@article{Umehara2010StructuralIF,
  title={Structural implications for K5/K12-di-acetylated histone H4 recognition by the second bromodomain of BRD2.},
  author={Takashi Umehara and Yoshihiro Nakamura and Masatoshi Wakamori and Keiko Ozato and Shigeyuki Yokoyama and Balasundaram Padmanabhan},
  journal={FEBS letters},
  year={2010},
  volume={584 18},
  pages={3901-8}
}
The BET family proteins recognize acetylated chromatin through their two bromodomains, acting as transcriptional activators or tethering viral genomes to the mitotic chromosomes of their host. The structural mechanism for how the N-terminal bromodomain of human BRD2 (BRD2-BD1) deciphers the mono-acetylated status of histone H4 tail was recently reported. Here we show the crystal structure of the second bromodomain of BRD2 (BRD2-BD2) in complex with the di-acetylated histone H4 tail (H4K5ac… CONTINUE READING

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