Secondary structure of a leucine zipper determined by nuclear magnetic resonance spectroscopy.

Journal Article

Previous work has shown that a synthetic peptide corresponding to the leucine zipper region of the yeast transcriptional activator GCN4 forms a stable dimer of alpha-helices and that the helices are oriented in a parallel manner. Two-dimensional nuclear magnetic resonance spectroscopy (NMR) is used here to demonstrate that the helix is continuous for at least 32 of the 33 residues in the peptide. The results also indicate that the dimer is symmetric. It is therefore unlikely that the interdigitation model for the structure of leucine zippers is correct, since interdigitation of leucine residues in a parallel dimer would lead to an asymmetric structure. The data are consistent with a coiled-coil structure.

Full Text

Duke Authors

Cited Authors

  • Oas, TG; McIntosh, LP; O'Shea, EK; Dahlquist, FW; Kim, PS

Published Date

  • March 27, 1990

Published In

Volume / Issue

  • 29 / 12

Start / End Page

  • 2891 - 2894

PubMed ID

  • 2337572

International Standard Serial Number (ISSN)

  • 0006-2960

Language

  • eng

Conference Location

  • United States