@article {2120,
	title = {Identification and structural characterization of a CBP/p300-binding domain from the ETS family transcription factor GABP alpha},
	journal = {Journal of Molecular Biology},
	volume = {377},
	number = {3},
	year = {2008},
	note = {ISI Document Delivery No.: 293ZPTimes Cited: 5Cited Reference Count: 60Kang, Hyun-Seo Nelson, Mary L. Mackereth, Cameron D. Scharpf, Manuela Graves, Barbara J. McIntosh, Lawrence P.},
	month = {Mar},
	pages = {636-646},
	type = {Article},
	abstract = {Using 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(x 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. (C) 2008 Elsevier Ltd. All rights reserved.},
	keywords = {BACKBONE DYNAMICS, C-13-LABELED PROTEINS, CREB-BINDING-PROTEIN, ESCHERICHIA-COLI, HIGH-RESOLUTION, HYPOXIA-INDUCIBLE FACTOR-1-ALPHA, LARGER PROTEINS, NEUROMUSCULAR-JUNCTION, NMR, NMR EXPERIMENTS, protein-protein interaction, RESIDUAL DIPOLAR COUPLINGS, SPECTROSCOPY, TRANSCRIPTION FACTOR, UBIQUITIN},
	isbn = {0022-2836},
	url = {<Go to ISI>://000255374200006},
	author = {Kang, H. S. and Nelson, M. L. and Mackereth, C. D. and Scharpf, M. and Graves, B. J. and McIntosh, L. P.}
}
