Fig. 7From: A novel interface between the N-terminal and coiled-coil domain of STAT1 functions in an auto-inhibitory mannerA novel mechanism for the dissociation of STAT1 from DNA through auto-inhibition. Surface representation of a tyrosine-phosphorylated parallel STAT1 dimer (yellow + green) binding to DNA (orange). The position of the respective N-terminal domains (N) is approximated. The critical amino acid position E169 (magenta) in the CCD is marked with arrows. According to the model, binding of the N-terminus to the E169 residue of its own core fragment facilitates dissociation from DNABack to article page