DNA binding by FOXP3 domain-swapped dimer suggests mechanisms of long-range chromosomal interactions

FOXP3 is a lineage-specific transcription factor that is required for regulatory T cell development and function. In this study, we determined the crystal structure of the FOXP3 forkhead domain bound to DNA. The structure reveals that FOXP3 can form a stable domain-swapped dimer to bridge DNA in the...

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Detalhes bibliográficos
Publicado no:Nucleic Acids Res
Main Authors: Chen, Yongheng, Chen, Chunxia, Zhang, Zhe, Liu, Chun-Chi, Johnson, Matthew E., Espinoza, Celso A., Edsall, Lee E., Ren, Bing, Zhou, Xianghong Jasmine, Grant, Struan F.A., Wells, Andrew D., Chen, Lin
Formato: Artigo
Idioma:Inglês
Publicado em: Oxford University Press 2015
Assuntos:
Structural Biology
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC4333414/
https://ncbi.nlm.nih.gov/pubmed/25567984
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1093/nar/gku1373
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