Characterization of bZIP protein binding specificities using a BACTH assay system

Basic leucine zipper domain (bZIP) transcription factors are proteins that dimerize to bind the promoter region of genes and control their expression. Interacting as classical helical coiled coils, the bZIP transcription factors exhibit the well-known pseudo- heptad repeat motif where every seventh residue is a leucine. Determination of the bZIP packing structure using the Knob-Socket (KS) model is a novel method to map the coiled-coil protein-protein interactions. The KS analysis and mapping has identified the residue sequences that may play a role in coiled-coil specificity