Crystal structure of the CENP-B protein-DNA complex: the DNA-binding domains of CENP-B induce kinks in the CENP-B box DNA.

@article{Tanaka2001CrystalSO,
  title={Crystal structure of the CENP-B protein-DNA complex: the DNA-binding domains of CENP-B induce kinks in the CENP-B box DNA.},
  author={Yoshinori Tanaka and Osamu Nureki and Hitoshi Kurumizaka and Shuya Fukai and Shin-Ichi Kawaguchi and Masahiro Ikuta and Junji Iwahara and Tuneko Okazaki and Shigeyuki Yokoyama},
  journal={The EMBO journal},
  year={2001},
  volume={20 23},
  pages={6612-8}
}
The human centromere protein B (CENP-B), one of the centromere components, specifically binds a 17 bp sequence (the CENP-B box), which appears in every other alpha-satellite repeat. In the present study, the crystal structure of the complex of the DNA-binding region (129 residues) of CENP-B and the CENP-B box DNA has been determined at 2.5 A resolution. The DNA-binding region forms two helix-turn-helix domains, which are bound to adjacent major grooves of the DNA. The DNA is kinked at the two… CONTINUE READING

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