Structural highlights
Function
[GABP2_MOUSE] Transcription factor capable of interacting with purine rich repeats (GA repeats). Must associate with GABP-alpha to bind DNA. [GABPA_MOUSE] Transcription factor capable of interacting with purine rich repeats (GA repeats).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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 Science. 1998 Feb 13;279(5353):1037-41. PMID:9461436[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Batchelor AH, Piper DE, de la Brousse FC, McKnight SL, Wolberger C. The structure of GABPalpha/beta: an ETS domain- ankyrin repeat heterodimer bound to DNA. Science. 1998 Feb 13;279(5353):1037-41. PMID:9461436
