2C6Y
Crystal structure of interleukin enhancer-binding factor 1 bound to DNA
Summary for 2C6Y
Entry DOI | 10.2210/pdb2c6y/pdb |
Related | 1JXS |
Descriptor | FORKHEAD BOX PROTEIN K2, INTERLEUKIN 2 PROMOTOR, MAGNESIUM ION, ... (5 entities in total) |
Functional Keywords | transcription regulation, dna-binding domain, forkhead transcription factors, interleukin enhancer binding factor, winged helix, forkhead |
Biological source | HOMO SAPIENS (HUMAN) More |
Cellular location | Nucleus (Probable): Q01167 |
Total number of polymer chains | 4 |
Total formula weight | 35466.10 |
Authors | Tsai, K.-L.,Huang, C.-Y.,Chang, C.-H.,Sun, Y.-J.,Chuang, W.-J.,Hsiao, C.-D. (deposition date: 2005-11-15, release date: 2006-04-18, Last modification date: 2024-05-08) |
Primary citation | Tsai, K.-L.,Huang, C.-Y.,Chang, C.-H.,Sun, Y.-J.,Chuang, W.-J.,Hsiao, C.-D. Crystal Structure of the Human Foxk1A-DNA Complex and its Implications on the Diverse Binding Specificity of Winged Helix/Forkhead Proteins. J.Biol.Chem., 281:17400-, 2006 Cited by PubMed Abstract: Interleukin 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. PubMed: 16624804DOI: 10.1074/JBC.M600478200 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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