@article {1233,
	title = {Variable control of Ets-1 DNA binding by multiple phosphates in an unstructured region},
	journal = {Science},
	volume = {309},
	number = {5731},
	year = {2005},
	note = {ISI Document Delivery No.: 941KDTimes Cited: 66Cited Reference Count: 30},
	month = {Jul},
	pages = {142-145},
	type = {Article},
	abstract = {Cell signaling that culminates in posttranslational modifications directs protein activity. Here we report how multiple Ca2+-dependent phosphorylation sites within the transcription activator Ets-1 act additively to produce graded DNA binding affinity. Nuclear magnetic resonance spectroscopic analyses show that phosphorylation shifts Ets-1 from a dynamic conformation poised to bind DNA to a well-folded inhibited state. These phosphates lie in an unstructured flexible region that functions as the allosteric effector of autoinhibition. Variable phosphorylation thus serves as a "rheostat" for cell signaling to fine-tune transcription at the level of DNA binding.},
	keywords = {allosteric regulation, AUTOINHIBITION, DOMAIN, DYNAMICS, NMR-SPECTROSCOPY, PHOSPHORYLATION, PROTEIN, SITES, TRANSACTIVATION, TRANSCRIPTION FACTOR NFAT1},
	isbn = {0036-8075},
	url = {<Go to ISI>://000230212800079},
	author = {Pufall, M. A. and Lee, G. M. and Nelson, M. L. and Kang, H. S. and Velyvis, A. and Kay, L. E. and McIntosh, L. P. and Graves, B. J.}
}
