R. Gentz, F.J. Rauscher III, C. Abate, T. Curran, "Parallel association of Fos and Jun leucine zippers juxtaposes DNA binding domains," Science, 243, 1695-99, 31 March 1989.
Tom Curran (Roche Institute of Molecular Biology, Nutley, N.J.): "The leucine zipper structure caught the imagination of scientists in several disciplines, not just those involved in transcriptional regulation. In this paper, we presented an extensive mutagenesis analysis of the oncogenes fos and jun, demonstrating that the leucine zipper mediates protein dimerization. Furthermore, we delineated a region of each protein rich in basic amino acids that constitutes the DNA- binding domain. The unique feature of this study was that we were able to compare the effects of mutations in both partners of a hetero- dimeric protein complex. This allowed us to predict that à helical regions of each interacted in a parallel configuration bringing into juxtaposition the DNA-binding domains. Thus, the leucine zipper has ...
