@article {3478,
	title = {MODULATION OF TRANSCRIPTION FACTOR ETS-1 DNA-BINDING - DNA-INDUCED UNFOLDING OF AN ALPHA-HELIX},
	journal = {Science},
	volume = {269},
	number = {5232},
	year = {1995},
	note = {ISI Document Delivery No.: RX194Times Cited: 143Cited Reference Count: 49},
	month = {Sep},
	pages = {1866-1869},
	type = {Article},
	abstract = {Conformational changes, including local protein folding, play important roles in protein-DNA interactions. Here, studies of the transcription factor Ets-1 provided evidence that local protein unfolding also can accompany DNA binding. Circular dichroism and partial proteolysis showed that the secondary structure of the Ets-1 DNA-binding domain is unchanged in the presence of DNA. In contrast, DNA allosterically induced the unfolding of an cr helix that lies within a flanking region involved in the negative regulation of DNA binding. These findings suggest a structural basis for the intramolecular inhibition of DNA binding and a mechanism for the cooperative partnerships that are common features of many eukaryotic transcription factors.},
	keywords = {BASIC REGION, CRYSTAL-STRUCTURE, DOMAIN, FAMILY, GCN4, INDUCED CONFORMATIONAL CHANGE, PROTEIN-KINASES, REPRESSOR, SEQUENCE, SUBUNITS},
	isbn = {0036-8075},
	url = {<Go to ISI>://A1995RX19400036},
	author = {Petersen, J. M. and Skalicky, J. J. and Donaldson, L. W. and McIntosh, L. P. and Alber, T. and Graves, B. J.}
}
