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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.
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P S Kim
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E K O'Shea, and
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October 1997,
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E K O'Shea, and
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E K O'Shea, and
R Rutkowski, and
P S Kim
February 2007,
Protein science : a publication of the Protein Society,
E K O'Shea, and
R Rutkowski, and
P S Kim
September 2021,
The Journal of biological chemistry,
E K O'Shea, and
R Rutkowski, and
P S Kim
February 2010,
Protein science : a publication of the Protein Society,
