@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.}
}
@article {389,
	title = {The solution structure and interactions of CheW from Thermotoga maritima},
	journal = {Nature Structural Biology},
	volume = {9},
	number = {2},
	year = {2002},
	note = {ISI Document Delivery No.: 516PHTimes Cited: 35Cited Reference Count: 34},
	month = {Feb},
	pages = {121-125},
	type = {Article},
	abstract = {Using protein from the hyperthermophile Thermotoga maritima, we have determined the solution structure of CheW, an essential component in the formation of the bacterial chemotaxis signaling complex. The overall fold is similar to the regulatory domain of the chemotaxis kinase CheA. In addition, interactions of CheW with CheA were monitored by nuclear magnetic resonance (NMR) techniques. The chemical shift perturbation data show the probable contacts that CheW makes with CheA. In combination with previous genetic data, the structure also suggests a possible binding site for the chemotaxis receptor. These results provide a structural basis for a model in which CheW acts as a molecular bridge between CheA and the cytoplasmic tails of the receptor.},
	keywords = {BACTERIAL CHEMOTAXIS, BINDING DOMAIN, C-13-LABELED PROTEINS, ESCHERICHIA-COLI, HISTIDINE KINASE, KINASE CHEA, NMR EXPERIMENTS, RESONANCE ASSIGNMENTS, SECONDARY STRUCTURE, SIGNAL-TRANSDUCTION},
	isbn = {1072-8368},
	url = {<Go to ISI>://000173562000015},
	author = {Griswold, I. J. and Zhou, H. J. and Matison, M. and Swanson, R. V. and McIntosh, L. P. and Simon, M. I. and Dahlquist, F. W.}
}
@article {4080,
	title = {Specific N-15,NH correlations for residues in N-15,C-13 and fractionally deuterated proteins that immediately follow methyl-containing amino acids},
	journal = {Journal of Biomolecular Nmr},
	volume = {10},
	number = {3},
	year = {1997},
	note = {ISI Document Delivery No.: YG934Times Cited: 10Cited Reference Count: 47},
	month = {Oct},
	pages = {283-288},
	type = {Article},
	abstract = {A triple-resonance pulse scheme is described which records N-15, NH correlations of residues that immediately follow a methyl-containing amino acid. The experiment makes use of a N-15, C-13 and fractionally deuterated protein sample and selects for CH2D methyl types. The experiment is thus useful in the early stages of the sequential assignment process as well as for the confirmation of backbone N-15, NH chemical shift assignments at later stages of data analysis. A simple modification of the sequence also allows the measurement of methyl side-chain dynamics. This is particularly useful for studying side-chain dynamic properties in partially unfolded and unfolded proteins where the resolution of aliphatic carbon and proton chemical shifts is limited compared to that of amide nitrogens.},
	keywords = {C-13, C-13/N-15-ENRICHED PROTEINS, CELLULOSE-BINDING DOMAIN, correlations, H-2 spin relaxation, H-2-labeled proteins, ISOTOPICALLY-ENRICHED PROTEINS, LABELED PROTEINS, N-15, NH, NMR EXPERIMENTS, PERDEUTERATED PROTEINS, RELAXATION-TIMES, SEQUENTIAL ASSIGNMENT, SIDE-CHAIN, TRIPLE-RESONANCE EXPERIMENTS},
	isbn = {0925-2738},
	url = {<Go to ISI>://A1997YG93400009},
	author = {Muhandiram, D. R. and Johnson, P. E. and Yang, D. W. and Zhang, O. W. and McIntosh, L. P. and Kay, L. E.}
}
