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Publication Abstract from PubMed

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 alpha-helix. This is the first study to report the presence of a C-terminal alpha-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.

Solution structure of the DNA-binding domain of interleukin enhancer binding factor 1 (FOXK1a).,Liu PP, Chen YC, Li C, Hsieh YH, Chen SW, Chen SH, Jeng WY, Chuang WJ Proteins. 2002 Dec 1;49(4):543-53. PMID:12402362^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.