Solution structure of the core NFATC1/DNA complex.

Published

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

Pubmed Central ID

  • 9506523

International Standard Serial Number (ISSN)

  • 0092-8674

Language

  • eng

Conference Location

  • United States