Controlling leucine zipper specificity with interfacial hydrophobic residues

Naresh P.S. Bains, Jackie A. Wilce, Lindsey G. Mackay, Glenn F. King

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5 Citations (Scopus)


Dimerisation of leucine zippers results from the parallel association of α-helices to form a coiled coil. Coiled coils comprise a heptad repeat, denoted as (abcdefg)(n), where residues at positions a and d are hydrophobic and constitute the core of the dimer interface. Charged amino acids at the e and g positions of the coiled coil are thought to be the major influence on dimerisation specificity through the formation of attractive and repulsive interhelical electrostatic interactions. However, the variability of a- position residues in leucine zipper transcription factors prompted us to investigate their influence on dimerisation specificity. We demonstrate that mutation of a single interfacial a-position Ala residue to either Val, Ile or Leu significantly alters the homo- and heterodimerisation specificities of the leucine zipper domain from the c-Jun transcription factor. These results illustrate the importance of a-position residues in controlling leucine zipper dimerisation specificity in addition to providing substantial contributions to dimer stability.

Original languageEnglish
Pages (from-to)381-390
Number of pages10
JournalLetters in Peptide Science
Issue number5-6
Publication statusPublished - 1 Jan 1999
Externally publishedYes


  • Coiled coil
  • Dimerisation affinity
  • Dimerisation specificity
  • Fos
  • Jun
  • Leucine zipper
  • Protein-protein interactions
  • Superzipper peptides

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