Solution structure of the core NFATC1/DNA complex.
Journal Article (Journal Article)
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.
Full Text
Duke Authors
Cited Authors
- Zhou, P; Sun, LJ; Dötsch, V; Wagner, G; Verdine, GL
Published Date
- March 6, 1998
Published In
Volume / Issue
- 92 / 5
Start / End Page
- 687 - 696
PubMed ID
- 9506523
International Standard Serial Number (ISSN)
- 0092-8674
Digital Object Identifier (DOI)
- 10.1016/s0092-8674(00)81136-8
Language
- eng
Conference Location
- United States