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1JXS

Solution Structure of the DNA-Binding Domain of Interleukin Enhancer Binding Factor

Summary for 1JXS
Entry DOI10.2210/pdb1jxs/pdb
NMR InformationBMRB: 4829
Descriptorinterleukin enhancer binding factor (1 entity in total)
Functional Keywordsdna-binding domain, winged helix, dna binding protein
Biological sourceHomo sapiens (human)
Cellular locationNucleus (Probable): Q01167
Total number of polymer chains1
Total formula weight11562.14
Authors
Chuang, W.J.,Liu, P.P.,Li, C.,Hsieh, Y.H.,Chen, S.W.,Chen, S.H.,Jeng, W.Y. (deposition date: 2001-09-08, release date: 2003-03-11, Last modification date: 2024-05-29)
Primary citationLiu, P.P.,Chen, Y.C.,Li, C.,Hsieh, Y.H.,Chen, S.W.,Chen, S.H.,Jeng, W.Y.,Chuang, W.J.
Solution structure of the DNA-binding domain of interleukin enhancer binding factor 1 (FOXK1a)
PROTEINS: STRUCT.,FUNCT.,GENET., 49:543-553, 2002
Cited by
PubMed 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.
PubMed: 12402362
DOI: 10.1002/prot.10227
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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