Foxp3 in Treg cell biology: a molecular and structural perspective

FOXP3 is the master transcription factor in regulating Treg cell development and function. The forkhead domain of FOXP3 forms a domain‐swapped dimer which can bridge two long‐range FOXP3‐targeted genes (a). The zinc‐finger and leucine‐zipper domain forms oligomerization through the hydrophobic coiled‐coil surface (b). Acetylation of K250 and K252 located in the coiled‐coil region changes the conformation of FOXP3, which implies a structure‐based regulation of the conformation and activity of FOXP3 by integration of posttranslational modifications may modulate Treg function. Understanding the molecular and structural features of Foxp3 helps to design rational therapeutic strategies against autoimmune diseases. Open in a separate window