Members of the basic leucine-zipper (bZIP) superfamily of transcription factors bind target DNA duplex sites as homodimers or heterodimers that recognize related but distinct palindromic sequences. The DNA-binding domain of bZIP transcription factors is the simplest known protein-DNA recognition motif and consists of a positively charged segment (basic region) linked to a sequence of heptad repeats of leucine residues (leucine zipper). bZIP family dimers form a chopsticks-like structure via dimerization of their leucine-zipper segments and each basic region segment contacts one-half of a palindromic site in the DNA major groove. bZIP transcription factors are effectors downstream of mitogenic stimulation, stress responses (oxidative, ER, heat), and cytokine stimulation. Additionally, the bZIP family of transcription factors affects several developmental processes including dendritic cell development, myeloid differentiation, and brain and ocular development.