The Structure of GABPα/β: An ETS Domain- Ankyrin Repeat Heterodimer Bound to DNA-Reference-Cited by-同舟云学术

The Structure of GABPα/β: An ETS Domain- Ankyrin Repeat Heterodimer Bound to DNA

Published:1998-02-13 Issue:5353 Volume:279 Page:1037-1041
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Batchelor Adrian H.¹²³,Piper Derek E.¹²³,de la Brousse Fabienne Charles¹²³,McKnight Steven L.¹²³,Wolberger Cynthia¹²³

Affiliation:

1. 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.

2. F. Charles de la Brousse, Tularik, Two Corporate Drive, South San Francisco, CA 94080, USA.

3. S. L. McKnight, Department of Biochemistry, University of Texas Southwestern Medical School, Dallas, TX 75235, USA.

Abstract

GA-binding protein (GABP) is a transcriptional regulator composed of two structurally dissimilar subunits. The α subunit contains a DNA-binding domain that is a member of the ETS family, whereas the β subunit contains a series of ankyrin repeats. The crystal structure of a ternary complex containing a GABPα/β 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 GABPα ETS domain binds to its core GGA DNA-recognition motif.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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