Structure of the DNA-binding domains from NFAT, Fos and Jun bound specifically to DNA (Q27748936)

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J N Glover

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P G Hogan

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A Rao

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S C Harrison

Signal transduction by lymphocyte antigen receptors

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language of work or name

English

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publication date

5 March 1998

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published in

Nature

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volume

392

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issue

6671

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page(s)

42-8

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cites work

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Signal transmission between the plasma membrane and nucleus of T lymphocytes

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Transcriptional regulation of the IL-2 gene

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The architecture of the interleukin-2 promoter: a reflection of T lymphocyte activation

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Identification of a putative regulator of early T cell activation genes

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Transcription factors of the NFAT family: regulation and function

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The mechanism of action of cyclosporin A and FK506

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Isolation of the cyclosporin-sensitive T cell transcription factor NFATp

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NF-AT components define a family of transcription factors targeted in T-cell activation

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NFATx, a novel member of the nuclear factor of activated T cells family that is expressed predominantly in the thymus

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The Rel family of eukaryotic transcription factors.

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Immunosuppressive drugs prevent a rapid dephosphorylation of transcription factor NFAT1 in stimulated immune cells

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Rapid shuttling of NF-AT in discrimination of Ca2+ signals and immunosuppression

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Role of kinases and the phosphatase calcineurin in the nuclear shuttling of transcription factor NF-AT4.

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Nuclear localization of NF-ATc by a calcineurin-dependent, cyclosporin-sensitive intramolecular interaction

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Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes

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Nuclear factor of activated T cells contains Fos and Jun.

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Human granulocyte-macrophage colony-stimulating factor enhancer function is associated with cooperative interactions between AP-1 and NFATp/c

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The T-cell transcription factor NFATp is a substrate for calcineurin and interacts with Fos and Jun

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Structure of the NF-kappa B p50 homodimer bound to DNA

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Structure of NF-kappa B p50 homodimer bound to a kappa B site

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Unusual Rel-like architecture in the DNA-binding domain of the transcription factor NFATc

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The GCN4 basic region leucine zipper binds DNA as a dimer of uninterrupted alpha helices: crystal structure of the protein-DNA complex

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The X-ray structure of the GCN4-bZIP bound to ATF/CREB site DNA shows the complex depends on DNA flexibility

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Crystal structure of the heterodimeric bZIP transcription factor c-Fos-c-Jun bound to DNA

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Sequence-specific recognition of double helical nucleic acids by proteins

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Transcription factors: structural families and principles of DNA recognition

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Dual role of the nuclear factor of activated T cells insert region in DNA recognition and cooperative contacts to activator protein 1.

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A critical arginine residue mediates cooperativity in the contact interface between transcription factors NFAT and AP-1

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Transcriptional activation: a complex puzzle with few easy pieces

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Determination of macromolecular structures from anomalous diffraction of synchrotron radiation

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Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons

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Only one of the two DNA-bound orientations of AP-1 found in solution cooperates with NFATp

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