TY - JOUR
T1 - The leucine zipper
T2 - A hypothetical structure common to a new class of DNA binding proteins
AU - Landschulz, William H.
AU - Johnson, Peter F.
AU - McKnight, Steven L.
PY - 1988
Y1 - 1988
N2 - 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 a 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 a helix interdigitate with those displayed from a similar a 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.
AB - 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 a 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 a helix interdigitate with those displayed from a similar a 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.
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U2 - 10.1126/science.3289117
DO - 10.1126/science.3289117
M3 - Article
C2 - 3289117
AN - SCOPUS:0024295767
SN - 0036-8075
VL - 240
SP - 1759
EP - 1764
JO - Science
JF - Science
IS - 4860
ER -