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Science 27 January 1989:
Vol. 243. no. 4890, pp. 538 - 542
DOI: 10.1126/science.2911757

Articles

Science, Vol 243, Issue 4890, 538-542
Copyright © 1989 by American Association for the Advancement of Science


articles

Evidence that the leucine zipper is a coiled coil

EK O'Shea, R Rutkowski, and PS Kim

Whitehead Institute for Biomedical Research, Cambridge, MA 02142.

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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Science. ISSN 0036-8075 (print), 1095-9203 (online)