X-ray scattering indicates that the leucine zipper is a coiled coil.
Proceedings of the National Academy of Sciences1991Vol. 88(2), pp. 561–564
Citations Over TimeTop 10% of 1991 papers
Abstract
Dimerization of the bZIP class of eukaryotic transcriptional control proteins requires a sequence motif called the leucine zipper. We have grown two distinct crystal forms of a 33-amino acid peptide corresponding to the leucine zipper of the yeast transcriptional activator GCN4. This peptide is known to form a dimer of parallel helices in solution. X-ray scattering from both crystal forms shows reflections that are diagnostic of coiled coils. The most notable reflections occur at approximately 5.2 A resolution and correspond to the pitch of helices in coiled coils. There is no diffraction maximum near 5.4 A, the characteristic pitch of straight helices. Our results provide direct evidence that the leucine zipper of GCN4 is a coiled coil.
Related Papers
- → Structure of the leucine zipper(1992)277 cited
- → The GCN4 leucine zipper can functionally substitute for the heat shock transcription factor’s trimerization domain(1997)33 cited
- 현사시나무에서 Basic Leucine Zipper 유전자의 분리와 특성 구명(2014)
- → Supplementary Figure 1 from Tumor-Suppressive Functions of Leucine Zipper Transcription Factor–Like 1(2023)