Crystal structure of an engrailed homeodomain-DNA complex at 2.8 A resolution: a framework for understanding homeodomain-DNA interactions.

@article{Kissinger1990CrystalSO,
  title={Crystal structure of an engrailed homeodomain-DNA complex at 2.8 A resolution: a framework for understanding homeodomain-DNA interactions.},
  author={Charles Kissinger and Bangtian Liu and E Mart{\'i}n-Blanco and Thomas B Kornberg and Carl O. Pabo},
  journal={Cell},
  year={1990},
  volume={63 3},
  pages={579-90}
}
The crystal structure of a complex containing the engrailed homeodomain and a duplex DNA site has been determined at 2.8 A resolution and refined to a crystallographic R factor of 24.4%. In this complex, two separate regions of the 61 amino acid polypeptide contact a TAAT subsite. An N-terminal arm fits into the minor groove, and the side chains of Arg-3 and Arg-5 make contacts near the 5' end of this "core consensus" binding site. An alpha helix fits into the major groove, and the side chains… CONTINUE READING

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