Display Settings:

Format

Send to:

Choose Destination

    Science. 1998 Feb 13;279(5353):1037-41.

    The structure of GABPalpha/beta: an ETS domain- ankyrin repeat heterodimer bound to DNA.

    Batchelor AH, Piper DE, de la Brousse FC, McKnight SL, Wolberger C.

    Department of Biophysics and Biophysical Chemistry and the Howard Hughes Medical Institute, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.

    Comment in:

    GA-binding protein (GABP) is a transcriptional regulator composed of two structurally dissimilar subunits. The alpha subunit contains a DNA-binding domain that is a member of the ETS family, whereas the beta subunit contains a series of ankyrin repeats. The crystal structure of a ternary complex containing a GABPalpha/beta ETS domain-ankyrin repeat heterodimer bound to DNA was determined at 2. 15 angstrom resolution. The structure shows how an ETS domain protein can recruit a partner protein using both the ETS domain and a carboxyl-terminal extension and provides a view of an extensive protein-protein interface formed by a set of ankyrin repeats. The structure also reveals how the GABPalpha ETS domain binds to its core GGA DNA-recognition motif.

    PMID: 9461436 [PubMed - indexed for MEDLINE]

    Supplemental Content

    Click here to read

    Structures reported by this article