Evidence that the leucine zipper is a coiled coil.
Recently, a hypothetical structure called a leucine zipper was proposed that defines a new class of DNA binding proteins. The common feature of these proteins is a region spanning approximately 30 amino acids that contains a periodic repeat of leucines every seven residues. A peptide corresponding to the leucine zipper region of the yeast transcriptional activator GCN4 was synthesized and characterized. This peptide associates in the micromolar concentration range to form a very stable dimer of alpha helices with a parallel orientation. Although some features of the leucine zipper model are supported by our experimental data, the peptide has the characteristics of a coiled coil.
O'Shea
E K
EK
Whitehead Institute for Biomedical Research, Cambridge, MA 02142.
Rutkowski
R
R
Kim
P S
PS
D000595:Amino Acid Sequence; D002851:Chromatography, High Pressure Liquid; D002942:Circular Dichroism; D004247:DNA / Q000378:metabolism; D004268:DNA-Binding Proteins; D004220:Disulfides; D005656:Fungal Proteins; D007930:Leucine; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D010446:Peptide Fragments; D011487:Protein Conformation; D011494:Protein Kinases; D012091:Repetitive Sequences, Nucleic Acid; D029701:Saccharomyces cerevisiae Proteins; D014157:Transcription Factors
D004268:DNA-Binding Proteins; D004220:Disulfides; D005656:Fungal Proteins; D046911:Macromolecular Substances; D010446:Peptide Fragments; D029701:Saccharomyces cerevisiae Proteins; D014157:Transcription Factors; D004247:DNA; D011494:Protein Kinases; D007930:Leucine