The structure of GABPalpha/beta: an ETS domain- ankyrin repeat heterodimer bound to DNA.
Batchelor, A.H., Piper, D.E., de la Brousse, F.C., McKnight, S.L., Wolberger, C.(1998) Science 279: 1037-1041
- PubMed: 9461436 
- DOI: https://doi.org/10.1126/science.279.5353.1037
- Primary Citation of Related Structures:  
1AWC - PubMed Abstract: 
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.
Organizational Affiliation: 
Department of Biophysics and Biophysical Chemistry and the Howard Hughes Medical Institute, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.