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    Proteins. 2002 Dec 1;49(4):543-53.

    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.

    Source

    Department of Biochemistry, National Cheng Kung University College of Medicine, Tainan 701, Taiwan.

    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.

    Copyright 2002 Wiley-Liss, Inc.

    PMID:
    12402362
    [PubMed - indexed for MEDLINE]

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