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Cell. 1998 Mar 6;92(5):687-96.

Solution structure of the core NFATC1/DNA complex.

Author information

1
Department of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts 02138, USA.

Abstract

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.

PMID:
9506523
DOI:
10.1016/s0092-8674(00)81136-8
[Indexed for MEDLINE]
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