1988/06/24 by William Landschulz, Peter F. Johnson, Steven L. McKnight · 10 citations
Biochemistry, Genetics and Molecular Biology · #Plant biochemistry and biosynthesis #Biochemical and Structural Characterization #Biotin and Related Studies
paper · doi:10.1126/science.3289117
openalex publication_date 1988/06/24 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/30
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 alpha 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 alpha-helical conformation, and the leucine side chains extending from one alpha helix interdigitate with those displayed from a similar alpha 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.