Solution structure of the DNA-binding domain of interleukin enhancer binding factor 1 (FOXK1a) |
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Authors: | Liu Pei-Phen Chen Yen-Chin Li Ching Hsieh Yu-Huei Chen Shu-Wan Chen Shu-Huei Jeng Wen-Yih Chuang Woei-Jer |
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Institution: | Department of Biochemistry, National Cheng Kung University College of Medicine, Tainan 701, Taiwan. |
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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 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. |
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