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| [[Image:2as5.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_2as5| PDB=2as5 | SCENE= }} | | {{STRUCTURE_2as5| PDB=2as5 | SCENE= }} |
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| '''Structure of the DNA binding domains of NFAT and FOXP2 bound specifically to DNA.'''
| | ===Structure of the DNA binding domains of NFAT and FOXP2 bound specifically to DNA.=== |
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| ==Overview==
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| Antigen stimulation of immune cells activates the transcription factor NFAT, a key regulator of T cell activation and anergy. NFAT forms cooperative complexes with the AP-1 family of transcription factors and regulates T cell activation-associated genes. Here we show that regulatory T cell (Treg) function is mediated by an analogous cooperative complex of NFAT with the forkhead transcription factor FOXP3, a lineage specification factor for Tregs. The crystal structure of an NFAT:FOXP2:DNA complex reveals an extensive protein-protein interaction interface between NFAT and FOXP2. Structure-guided mutations of FOXP3, predicted to progressively disrupt its interaction with NFAT, interfere in a graded manner with the ability of FOXP3 to repress expression of the cytokine IL2, upregulate expression of the Treg markers CTLA4 and CD25, and confer suppressor function in a murine model of autoimmune diabetes. Thus by switching transcriptional partners, NFAT converts the acute T cell activation program into the suppressor program of Tregs.
| | The line below this paragraph, {{ABSTRACT_PUBMED_16873067}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 16873067 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_16873067}} |
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| ==Disease== | | ==Disease== |
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| [[Category: Rhr domain]] | | [[Category: Rhr domain]] |
| [[Category: Winged helix-turn-helix]] | | [[Category: Winged helix-turn-helix]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:24:50 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 04:47:58 2008'' |