Summary information and primary citation
- PDB-id
-
1a66;
DSSR-derived features in text and
JSON formats; DNAproDB
- Class
- transcription-DNA
- Method
- NMR
- Summary
- Solution NMR structure of the core nfatc1-DNA complex,
18 structures
- Reference
-
Zhou P, Sun LJ, Dotsch V, Wagner G, Verdine GL (1998):
"Solution
structure of the core NFATC1/DNA complex."
Cell(Cambridge,Mass.), 92,
687-696. doi: 10.1016/S0092-8674(00)81136-8.
- 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.
