The nuclear factor of the activated T cell (NFAT) family of transcription factors regulates cytokine gene expression by binding to the promoter/enhancer regions of antigen-responsive genes, usually in cooperation with heterologous DNA-binding partners. Here we report the solution structure of the binary complex formed between the core DNA-binding domain of human NFATC1 and the ARRE2 DNA site from the interleukin-2 promoter. The structure reveals that DNA binding induces the folding of key structural elements that are required for both sequence-specific recognition and the establishment of cooperative protein-protein contacts. The orientation of the NFAT DNA- binding domain observed in the binary NFATC1-DBD/DNA complex is distinct from that seen in the ternary NFATC2/AP-1/DNA complex, suggesting that the domain reorients upon formation of a cooperative transcriptional complex.
Zhou, P., Sun, L. J., Dötsch, V., Wagner, G., & Verdine, G. L. (1998). Solution structure of the core NFATC1/DNA complex. Cell, 92(5), 687–696. https://doi.org/10.1016/S0092-8674(00)81136-8