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Structural basis of Hox specificity

Nature Structural Biology volume 6, pages 297–300 (1999)Cite this article

Abstract

On their own, the homeotic selector (Hox) transcriptional regulators bind very short, rather similar DNA sequences. To elevate their functional specificity, Hox proteins heterodimerize with other homeodomain-containing proteins. The structural basis for this fruitful partnership is now coming into view.

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Figure 1: The Hox–PBC consensus DNA recognition sequence and the preference of different Hox genes for the sixth position of the consensus.
Figure 2: The HoxB1–Pbx1–DNA complex20.
Figure 3: The hexapeptide–PBC interaction.
Figure 4: Comparative anatomy of structurally characterized dimeric HD structures on DNA.

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Acknowledgements

We thank C. Wolberger and A. Aggarwal for sharing coordinates prior to publication. Thanks also to G. Zimmermann and M. Phelan for commenting on the manuscript and to G. Zimmermann, J. Urbach and J. Davis for help with figures.

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Authors and Affiliations

  1. David Wilson and Claude Desplan are in the Howard Hughes Medical Institute.,

    David S. Wilson & Claude Desplan

  2. Massachusetts General Hospital, Boston, 02114, Massachusetts, USA

    David S. Wilson

  3. The Rockefeller University, New York, 10021, New York, USA

    Claude Desplan

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  1. David S. Wilson
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  2. Claude Desplan
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Correspondence to David S. Wilson.

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Wilson, D., Desplan, C. Structural basis of Hox specificity. Nat Struct Mol Biol 6, 297–300 (1999). https://doi.org/10.1038/7524

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