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Science 25 October 1991: Vol. 254. no. 5031, pp. 539 - 544 DOI: 10.1126/science.1948029
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Articles
Science, Vol 254, Issue 5031, 539-544
Copyright © 1991 by American Association for the Advancement of Science
X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil
EK O'Shea,
JD Klemm,
PS Kim,
and
T Alber
Howard Hughes Medical Institute, Cambridge, MA 02142.
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 alpha 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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- Multimer Formation Is Not Essential for Nuclear Export of Human T-Cell Leukemia Virus Type 1 Rex trans-Activator Protein.
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