Solution structure of the DNA-binding domain of interleukin enhancer binding factor 1 (FOXK1a)

Pei Phen Liu, Yen Chin Chen, Ching Li, Yu Huei Hsieh, Shu Wan Chen, Shu Huei Chen, Wen Yih Jeng, Woei Jer Chuang

Research output: Contribution to journalArticlepeer-review

18 Citations (Scopus)

Abstract

Interleukin enhancer binding factor (ILF) binds to the interleukin-2 (IL-2) promoter and regulates IL-2 gene expression. In this study, the 3D structure of the DNA-binding domain of ILF was determined by multidimensional NMR spectroscopy. NMR structure analysis revealed that the DNA-binding domain of ILF is a new member of the winged helix/forkhead family, and that its wing 2 contains an extra α-helix. This is the first study to report the presence of a C-terminal α-helix in place of a typical wing 2 in a member of this family. This structural difference may be responsible for the different DNA-binding specificity of ILF compared to other winged helix/forkhead proteins. Our deletion studies of the fragments of ILF also suggest that the C-terminal region plays a regulatory role in DNA binding.

Original languageEnglish
Pages (from-to)543-553
Number of pages11
JournalProteins: Structure, Function and Genetics
Volume49
Issue number4
DOIs
Publication statusPublished - 2002 Dec 1

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Biochemistry
  • Molecular Biology

Fingerprint Dive into the research topics of 'Solution structure of the DNA-binding domain of interleukin enhancer binding factor 1 (FOXK1a)'. Together they form a unique fingerprint.

Cite this