@article {3657,
	title = {Solution structure of the ETS domain from murine Ets-1: A winged helix-turn-helix DNA binding motif},
	journal = {Embo Journal},
	volume = {15},
	number = {1},
	year = {1996},
	note = {ISI Document Delivery No.: TQ160Times Cited: 113Cited Reference Count: 68},
	month = {Jan},
	pages = {125-134},
	type = {Article},
	abstract = {Ets-1 is the prototypic member of the ets family of transcription factors, This family is characterized by the conserved ETS domain that mediates specific DNA binding, Using NMR methods, we have determined the structure of a fragment of murine Ets-1 composed of the 85 residue ETS domain and a 25 amino acid extension that ends at its native C-terminus. The ETS domain folds into a helix-turn-helix moth on a four-stranded anti-parallel beta-sheet scaffold. This structure places Ets-1 in the winged helix-turn-helix (wHTH) family of DNA binding proteins and provides a model for interpreting the sequence conservation of the ETS domain and the specific interaction of Ets-1 with DNA. The C-terminal sequence of Ets-1, which is mutated in the v-Ets oncoprotein, forms an alpha-helix that packs anti-parallel to the N-terminal helix of the ETS domain, In this position, the C-terminal helix is poised to interact directly with an N-terminal inhibitory region in Ets-1 as well as the wHTH motif. This explains structurally the concerted role of residues flanking the ETS domain in the intramolecular inhibition of Ets-1 DNA binding.},
	keywords = {AMINO-ACID SUBSTITUTION, C-13, C-ETS-1, COUPLING-CONSTANTS, CRYSTAL-STRUCTURE, DNA binding, ERYTHROBLASTOSIS, FACTORS, GENE FAMILY, intramolecular inhibition, protein NMR structure, PROTEINS, selective labelling, transcription, V-ETS, winged helix-turn-helix},
	isbn = {0261-4189},
	url = {<Go to ISI>://A1996TQ16000013},
	author = {Donaldson, L. W. and Petersen, J. M. and Graves, B. J. and McIntosh, L. P.}
}
@article {3819,
	title = {Structural coupling of the inhibitory regions flanking the ETS domain of murine Ets-1},
	journal = {Protein Science},
	volume = {5},
	number = {2},
	year = {1996},
	note = {ISI Document Delivery No.: TU724Times Cited: 46Cited Reference Count: 66},
	month = {Feb},
	pages = {296-309},
	type = {Article},
	abstract = {Several members of the ets gene family of transcription factors show negative regulation of DNA binding by intramolecular interactions. A structural mechanism for this auto-inhibition is investigated using a 161-residue N-terminal deletion mutant of murine Ets-1, Ets-1 Delta N280. This protein shows a similar reduced affinity for DNA as native Ets-1 because it contains the ETS domain in context of the flanking amino- and carboxy-terminal regions that together mediate repression of DNA binding. The secondary structure of Ets-1 Delta N280 was determined using NMR chemical shift, NOE, J coupling, and amide hydrogen exchange information. In addition to the winged helix-turn-helix ETS domain, Ets-1 Delta N280 contains two alpha-helices in the amino-terminal inhibitory region and one alpha-helix in the carboxy-terminal inhibitory region. Chemical shift comparisons were made between this protein and an activated form of Ets-1 lacking the amino-terminal inhibitory region. The spectral differences demonstrate that the amino- and carboxy-terminal inhibitory sequences are structurally coupled to one another, thus explaining the observation that both regions are required for the repression of DNA binding. Furthermore, these data show that the inhibitory sequences also interact directly with the first helix of the intervening ETS domain, thereby providing a pathway for the repression of DNA binding. These results lead to a model of an inhibitory module in Ets-1 composed of both the amino- and carboxy-terminal regions interfaced with the ETS domain. This establishes the structural framework for understanding the intramolecular inhibition of Ets-1 DNA binding.},
	keywords = {3-DIMENSIONAL NMR-SPECTROSCOPY, allosteric, ASSIGNMENT, CRYSTAL-STRUCTURE, DNA binding, DNA-BINDING MOTIF, ETS domain, Ets-1 and Ets-2, FACTORS, H-1, INHIBITION, INTRAMOLECULAR, LARGER PROTEINS, N-15 NMR, NMR, protein structure, SPECTRA, transcription, V-ETS, winged helix-turn-helix},
	isbn = {0961-8368},
	url = {<Go to ISI>://A1996TU72400014},
	author = {Skalicky, J. J. and Donaldson, L. W. and Petersen, J. M. and Graves, B. J. and McIntosh, L. P.}
}
