The structure of GABPα/β: 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

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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 α 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.

Original languageEnglish (US)
Pages (from-to)1037-1041
Number of pages5
JournalScience
Volume279
Issue number5353
DOIs
Publication statusPublished - Feb 13 1998

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Cite this

Batchelor, A. H., Piper, D. E., Charles De La Brousse, F., McKnight, S. L., & Wolberger, C. (1998). The structure of GABPα/β: An ETS domain-ankyrin repeat heterodimer bound to DNA. Science, 279(5353), 1037-1041. https://doi.org/10.1126/science.279.5353.1037