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A critical arginine residue mediates cooperativity in the contact interface between transcription factors NFAT and AP-1.
The leucine zipper domain controls the orientation of AP-1 in the NFAT.AP-1.DNA complex.
Dual role of the nuclear factor of activated T cells insert region in DNA recognition and cooperative contacts to activator protein 1.
The orientation of the AP-1 heterodimer on DNA strongly affects transcriptional potency.
Unusual Rel-like architecture in the DNA-binding domain of the transcription factor NFATc.
Only one of the two DNA-bound orientations of AP-1 found in solution cooperates with NFATp.
Transcription Factor AP-1
Transcription Factor AP 2