Figure 2.

Schematic diagram of IRF4 structure. IRF4 consists of three structural domains: a highly conserved N-terminal DNA-binding domain (DBD), a variable C-terminal IRF association domain (IAD) and an intermediate linker domain (ILD). The DBD is characterized by five conserved tryptophans enabling it to form a helix–loop–helix motif that facilitates DNA binding. IAD is a protein–protein interaction domain that mediates the interaction of IRF4 with itself or multiple distinct transcription factors. IAD also contains a C-terminal auto-inhibitory region (AR) which physically interacts with DBD and results in low DNA binding affinity.