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X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil.

O'Shea EK, Klemm JD, Kim PS, Alber T
Science 254 539-44 (1991)
Cited: 838 times
EuropePMC logo PMID: 1948029

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 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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Related citations provided by authors (2)

  1. X-ray scattering indicates that the leucine zipper is a coiled coil.. Rasmussen R, Benvegnu D, O'Shea EK, Kim PS, Alber T Proc Natl Acad Sci U S A 88 561-4 (1991)
  2. Evidence that the Leucine Zipper is a Coiled Coil. O'Shea EK, Rutkowski R, Kim PS Science 243 538- (1989)

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