The Leucine Zipper: A Hypothetical Structure Common to a New Class of DNA Binding Proteins

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  • William H. Landschulz
    Department of Embryology, Carnegie Institution of Washington, Baltimore, MD 21210.
  • Peter F. Johnson
    Department of Embryology, Carnegie Institution of Washington, Baltimore, MD 21210.
  • Steven L. McKnight
    Department of Embryology, Carnegie Institution of Washington, Baltimore, MD 21210.

Bibliographic Information

Published
1988-06-24
DOI
  • 10.1126/science.3289117
Publisher
American Association for the Advancement of Science (AAAS)

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Description

<jats:p>A 30-amino-acid segment of C/EBP, a newly discovered enhancer binding protein, shares notable sequence similarity with a segment of the cellular Myc transforming protein. Display of these respective amino acid sequences on an idealized α helix revealed a periodic repetition of leucine residues at every seventh position over a distance covering eight helical turns. The periodic array of at least four leucines was also noted in the sequences of the Fos and Jun transforming proteins, as well as that of the yeast gene regulatory protein, GCN4. The polypeptide segments containing these periodic arrays of leucine residues are proposed to exist in an α-helical conformation, and the leucine side chains extending from one α helix interdigitate with those displayed from a similar α helix of a second polypeptide, facilitating dimerization. This hypothetical structure is referred to as the "leucine zipper," and it may represent a characteristic property of a new category of DNA binding proteins.</jats:p>

Journal

  • Science

    Science 240 (4860), 1759-1764, 1988-06-24

    American Association for the Advancement of Science (AAAS)

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