Abstract
The x-ray crystal structure of a peptide corresponding to the leucine zipper of the yeast transcriptional activator GCN4 has been determined at 1.8 angstrom resolution. The peptide forms a parallel, two-stranded coiled coil of α helices packed as in the "knobs-into-holes" model proposed by Crick in 1953. Contacts between the helices include ion pairs and an extensive hydrophobic interface that contains a distinctive hydrogen bond. The conserved leucines, like the residues in the alternate hydrophobic repeat, make side-to-side interactions (as in a handshake) in every other layer of the dimer interface. The crystal structure of the GCN4 leucine zipper suggests a key role for the leucine repeat, but also shows how other features of the coiled coil contribute to dimer formation.
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Dates
Type | When |
---|---|
Created | 18 years, 10 months ago (Oct. 5, 2006, 6:10 p.m.) |
Deposited | 1 year, 7 months ago (Jan. 11, 2024, 5:10 p.m.) |
Indexed | 1 day, 6 hours ago (Aug. 21, 2025, 1:55 p.m.) |
Issued | 33 years, 9 months ago (Oct. 25, 1991) |
Published | 33 years, 9 months ago (Oct. 25, 1991) |
Published Print | 33 years, 9 months ago (Oct. 25, 1991) |
@article{O_Shea_1991, title={X-Ray Structure of the GCN4 Leucine Zipper, a Two-Stranded, Parallel Coiled Coil}, volume={254}, ISSN={1095-9203}, url={http://dx.doi.org/10.1126/science.1948029}, DOI={10.1126/science.1948029}, number={5031}, journal={Science}, publisher={American Association for the Advancement of Science (AAAS)}, author={O’Shea, Erin K. and Klemm, Juli D. and Kim, Peter S. and Alber, Tom}, year={1991}, month=oct, pages={539–544} }