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Solution structure of the ets domain of Fli-1 when bound to DNA

Nature Structural Biology volume 1, pages 871–876 (1994)Cite this article

Abstract

Members of the ets family of transcription factors share a conserved DNA-binding domain, the ets domain. By using multidimensional NMR, we have determined the structure of the ets domain of human Fli-1 in the DNA-bound form. It consists of three α-helices and a four-stranded β-sheet, similar to structures of the class of helix-turn-helix DNA binding proteins first found in the catabolite activator protein of Escherichia coli. NMR and mutagenesis experiments suggest that in comparison to structurally related proteins, the ets domain uses a new variation of the helix-turn-helix motif for binding to DNA.

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Authors and Affiliations

  1. Pharmaceutical Discovery Division, Abbott Laboratories, Abbott Park, Illinois, 60064, USA

    Heng Liang, Edward T. Olejniczak, David G. Nettesheim, Liping Yu, Robert P. Meadows & Stephen W. Fesik

  2. Howard Hughes Medical Institute and Department of Molecular Genetics and Cell Biology, The University of Chicago, Illinois, 60637, USA

    Xiaohong Mao & Craig B. Thompson

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  1. Heng Liang
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Liang, H., Mao, X., Olejniczak, E. et al. Solution structure of the ets domain of Fli-1 when bound to DNA. Nat Struct Mol Biol 1, 871–876 (1994). https://doi.org/10.1038/nsb1294-871

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