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Fig. 1. (A) Domain organization of C/EBP-family members. Each C/EBP protein contains a functionally related leucine zipper dimerization domain (LZ) at its C-terminus. All family members, with the exception of C/EBP ${zeta}$ , share an adjacent highly conserved basic region (BR) that mediates sequence-specific DNA binding. C/EBP ${alpha}$ , C/EBPß, C/EBP ${delta}$ and C/EBP ${epsilon}$ each contain transactivation domains (TADs) and a regulatory domain (RD) located in their N-terminal regions. A tripartite TAD at the N-terminus displays homology among several of the family members (Williams et al., 1995). (B) The predicted structure of a C/EBP bZIP dimer bound to its cognate DNA site.

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