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pubmed-article:16624804pubmed:abstractTextInterleukin enhancer binding factor (ILF) is a human transcription factor and a new member of the winged helix/forkhead family. ILF can bind to purine-rich regulatory motifs such as the human T-cell leukemia virus-long terminal region and the interleukin-2 promoter. Here we report the 2.4 A crystal structure of two DNA binding domains of ILF (FOXK1a) binding to a 16-bp DNA duplex containing a promoter sequence. Electrophoretic mobility shift assay studies demonstrate that two ILF-DNA binding domain molecules cooperatively bind to DNA. In addition to the recognition helix recognizing the core sequences through the major groove, the structure shows that wing 1 interacts with the minor groove of DNA, and the H2-H3 loop region makes ionic bonds to the phosphate group, which permits the recognition of DNA. The structure also reveals that the presence of the C-terminal alpha-helix in place of a typical wing 2 in a member of this family alters the orientation of the C-terminal basic residues (RKRRPR) when binding to DNA outside the core sequence. These results provide a new insight into how the DNA binding specificities of winged helix/forkhead proteins may be regulated by their less conserved regions.lld:pubmed
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pubmed-article:16624804pubmed:authorpubmed-author:SunYuh-JuYJlld:pubmed
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pubmed-article:16624804pubmed:dateRevised2008-11-21lld:pubmed
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pubmed-article:16624804pubmed:articleTitleCrystal structure of the human FOXK1a-DNA complex and its implications on the diverse binding specificity of winged helix/forkhead proteins.lld:pubmed
pubmed-article:16624804pubmed:affiliationInstitute of Molecular Biology, Academia Sinica, Taipei 115, Taiwan.lld:pubmed
pubmed-article:16624804pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:16624804pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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