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Article

Structure of a domain-swapped FOXP3 dimer on DNA and its function in regulatory T cells.

Immunity - 22 Apr 2011

Bandukwala Hozefa S, Wu Yongqing, Feuerer Markus, Chen Yongheng, Barboza Bianca, Ghosh Srimoyee, Stroud James C, Benoist Christophe, Mathis Diane, Rao Anjana, Chen Lin

Abstract excerpt

The transcription factor FOXP3 is essential for the suppressive function of regulatory T cells that are required for maintaining self-tolerance. We have solved the crystal structure of the FOXP3 forkhead domain as a ternary complex with the DNA-binding domain of the transcription factor NFAT1 and a DNA oligonucleotide from the interleukin-2 promoter. A striking feature of this structure is that FOXP3 forms a...

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Share to Forkhead Transcription Factors
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Share to Protein Multimerization

Share to Protein Structure, Quaternary

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Share to T-Lymphocytes, Regulatory

Source

Open in PubMed Open full text

Identifiers

PMID: 21458306
DOI: 10.1016/j.immuni.2011.02.017
PMCID: PMC3085397

Genes

FOXP3

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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