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Science 13 February 1998:
Vol. 279. no. 5353, pp. 1037 - 1041
DOI: 10.1126/science.279.5353.1037
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Reports

The Structure of GABPalpha /beta : An ETS Domain- Ankyrin Repeat Heterodimer Bound to DNA

Adrian H. Batchelor, Derek E. Piper, Fabienne Charles de la Brousse, Steven L. McKnight, Cynthia Wolberger *

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.

A. H. Batchelor, D. E. Piper, C. Wolberger, Department of Biophysics and Biophysical Chemistry and the Howard Hughes Medical Institute, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
F. Charles de la Brousse, Tularik, Two Corporate Drive, South San Francisco, CA 94080, USA.
S. L. McKnight, Department of Biochemistry, University of Texas Southwestern Medical School, Dallas, TX 75235, USA.
*   To whom correspondence should be addressed. E-mail: cynthia{at}groucho.med.jhmi.edu

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