1A66

SOLUTION NMR STRUCTURE OF THE CORE NFATC1/DNA COMPLEX, 18 STRUCTURES

Summary for 1A66

• Entry DOI: 10.2210/pdb1a66/pdb
• Descriptor: DNA (5'-D(*CP*GP*AP*GP*GP*AP*AP*AP*AP*TP*TP*G)-3'), DNA (5'-D(*CP*AP*AP*TP*TP*TP*TP*CP*CP*TP*CP*G)-3'), CORE NFATC1 (3 entities in total)
• Functional Keywords: nfatc1/dna, rel, nfat/dna, arre2, nfat, nfatc1, nfatc, nfat2, binary complex, transcription factor, enhanceosome, il-2, complex, binary, transcription-dna complex, transcription/dna
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: O95644
• Total number of polymer chains: 3
• Total formula weight: 27328.72

Authors

Zhou, P.,Sun, L.J.,Doetsch, V.,Wagner, G.,Verdine, G.L. (deposition date: 1998-03-06, release date: 1998-06-17, Last modification date: 2024-05-22)

Primary citation

Zhou, P.,Sun, L.J.,Dotsch, V.,Wagner, G.,Verdine, G.L.
Solution structure of the core NFATC1/DNA complex.
Cell(Cambridge,Mass.), 92:687-696, 1998

PubMed 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.

PubMed: 9506523
DOI: 10.1016/S0092-8674(00)81136-8

Experimental method

SOLUTION NMR