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Solution structure of the core NFATC1/DNA complex.

P Zhou·L J Sun·V Dötsch·G Wagner·G L Verdine
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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.

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Amino Acid SequenceDNADNA-Binding ProteinsEnhancer Elements, GeneticHumansInterleukin-2Models, MolecularMolecular Sequence DataNFATC Transcription FactorsNuclear Magnetic Resonance, BiomolecularNuclear ProteinsNucleic Acid ConformationOligodeoxyribonucleotidesPoint MutationProtein ConformationSequence AlignmentTranscription FactorsJournal ArticleResearch Support, Non-U.S. Gov'tResearch Support, U.S. Gov't, Non-P.H.S.Research Support, U.S. Gov't, P.H.S.

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P Zhou, L J Sun, V Dötsch, G Wagner, G L Verdine. 1998-03-06. Solution structure of the core NFATC1/DNA complex.. https://doi.org/10.1016/s0092-8674(00)81136-8

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