User:Mbennie/Notebook/Papers and Books/Leucine Zippers

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  1. Ramji DP and Foka P. CCAAT/enhancer-binding proteins: structure, function and regulation. Biochem J. 2002 Aug 1;365(Pt 3):561-75. DOI:10.1042/BJ20020508 | PubMed ID:12006103 | HubMed [CCAAT-Review]


  1. Newman JR and Keating AE. Comprehensive identification of human bZIP interactions with coiled-coil arrays. Science. 2003 Jun 27;300(5628):2097-101. DOI:10.1126/science.1084648 | PubMed ID:12805554 | HubMed [Identification-bZIP]
  • Characterizes interactions between 49 leucine zippers using protein arrays
  • Observed that families make similar interactions
  • Observed high symmetry
  • Figure 2 of this paper shows interactions between 49 leucine zippers, color-coated by strength

Family Alignment for the BRLZ domain

  • Click "Family Alignment" to see list of leucine zippers
  • Might be useful in locating sequence information for various leucine zippers


  1. Grigoryan G and Keating AE. Structure-based prediction of bZIP partnering specificity. J Mol Biol. 2006 Feb 3;355(5):1125-42. DOI:10.1016/j.jmb.2005.11.036 | PubMed ID:16359704 | HubMed [Predicting-bZIP-interactions]
  • Leucine zippers have (abcdefg)n repeat - zippers interface with a, d, e, and g residues
  • Mostly computational information - predicting results generated by Comprehensive Identification of Human bZIP paper


  1. Vinson CR, Sigler PB, and McKnight SL. Scissors-grip model for DNA recognition by a family of leucine zipper proteins. Science. 1989 Nov 17;246(4932):911-6. DOI:10.1126/science.2683088 | PubMed ID:2683088 | HubMed [Scissors-Grip-Model]
  • Leucine zippers are Y-shaped, recognize binding sites on DNA
  • "Dimer-forming region...hypothesized to consist of two amphipathic alpha helices, about 30 amino acids long, that adhere tightly to one another through a narrow hydrophobic spine punctuated every seven residues by a leucine side chain."
  • N-terminus side responsible for DNA binding
  • basic region-leucine zipper -> bZIP
  • DNA targets are "directly abutted, inverted repeats"


  1. Landschulz WH, Johnson PF, and McKnight SL. The leucine zipper: a hypothetical structure common to a new class of DNA binding proteins. Science. 1988 Jun 24;240(4860):1759-64. DOI:10.1126/science.3289117 | PubMed ID:3289117 | HubMed [Leucinezipper-Early]
  • Introduces leucine zipper, information about similar methods of gene regulation: helix-turn-helix and zinc fingers
  • Compares several leucine zippers and identifies patterns (mainly leucine every seven aa)
  • Explains physical properties of leucine that make it ideal candidate for this role