Buried polar residues and structural specificity in the GCN4 leucine zipper

@article{Gonzalez1996BuriedPR,
  title={Buried polar residues and structural specificity in the GCN4 leucine zipper},
  author={Lino Gonzalez and Derek N. Woolfson and Tom Alber},
  journal={Nature Structural Biology},
  year={1996},
  volume={3},
  pages={1011-1018}
}
A conserved asparagine (Asn 16) buried in the interface of the GCN4 leucine zipper selectively favours the parallel, dimeric, coiled-coil structure. To test if other polar residues confer oligomerization specificity, the structural effects of Gin and Lys substitutions for Asn 16 were characterized. Like the wild-type peptide, the Asn16Lys mutant formed exclusively dimers. In contrast. Gin 16, despite its chemical similarity to Asn, allowed the peptide to form both dimers and trimers. The Gin 16… CONTINUE READING