2juo
GABPa OST domain
Structural highlights
FunctionGABPA_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 PubMedUsing NMR spectroscopy, we identified and characterized a previously unrecognized structured domain near the N-terminus (residues 35-121) of the ETS family transcription factor GABP alpha. The monomeric domain folds as a five-stranded beta-sheet crossed by a distorted helix. Although globally resembling ubiquitin, the GABP alpha fragment differs in its secondary structure topology and thus appears to represent a new protein fold that we term the OST (On-SighT) domain. The surface of the GABP alpha OST domain contains two predominant clusters of negatively-charged residues suggestive of electrostatically driven interactions with positively-charged partner proteins. Following a best-candidate approach to identify such a partner, we demonstrated through NMR-monitored titrations and glutathione S-transferase pulldown assays that the OST domain binds to the CH1 and CH3 domains of the co-activator histone acetyltransferase CBP/p300. This provides a direct structural link between GABP and a central component of the transcriptional machinery. Identification and structural characterization of a CBP/p300-binding domain from the ETS family transcription factor GABP alpha.,Kang HS, Nelson ML, Mackereth CD, Scharpf M, Graves BJ, McIntosh LP J Mol Biol. 2008 Mar 28;377(3):636-46. Epub 2008 Jan 30. PMID:18295234[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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