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Recognition by Max of its cognate DNA through a dimeric b/HLH/Z domain

Nature volume 363, pages 38–45 (1993)Cite this article

Abstract

The three-dimensional structure of the basic/helix–loop–helix/leucine zipper domain of the transcription factor Max complexed with DNA has been determined by X-ray crystallography at 2.9 Å resolution. Max binds as a dimer to its recognition sequence CACGTG by direct contacts between the α-helical basic region and the major groove. This symmetric homodimer, a new protein fold, is a parallel, left-handed, four-helix bundle, with each monomer containing two α-helical segments separated by a loop. The two α-helical segments are composed of the basic region plus helix 1 and helix 2 plus the leucine repeat, respectively. As in GCN4, the leucine repeat forms a parallel coiled coil.

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Author notes

  1. George C. Prendergast

    Present address: Merck Research Laboratories, Department of Cancer Research, West Point, Pennsylvania, 19486, USA

  2. Stephen K. Burley: To whom correspondence should be addressed.

Authors and Affiliations

  1. Laboratories of Molecular Biophysics, The Rockefeller University, 1230 York Avenue, New York, New York, 10021, USA

    Adrian R. Ferré-D'Amaré & Stephen K. Burley

  2. Howard Hughes Medical Institute, The Rockefeller University, 1230 York Avenue, New York, New York, 10021, USA

    Stephen K. Burley

  3. Department of Biochemistry, Kaplan Cancer Center, New York University Medical Center, New York, New York, 10016, USA

    George C. Prendergast & Edward B. Ziff

  4. Howard Hughes Medical Institute, New York University Medical Center, New York, New York, 10016, USA

    Edward B. Ziff

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  1. Adrian R. Ferré-D'Amaré
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  3. Edward B. Ziff
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  4. Stephen K. Burley
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Ferré-D'Amaré, A., Prendergast, G., Ziff, E. et al. Recognition by Max of its cognate DNA through a dimeric b/HLH/Z domain. Nature 363, 38–45 (1993). https://doi.org/10.1038/363038a0

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