@article {2417,
	title = {Distinct conformational states of nuclear receptor-bound CRSP-Med complexes.},
	journal = {Nature Structural \& Molecular Biology},
	volume = {11},
	year = {2004},
	month = {2004 Jul},
	pages = {664-71},
	abstract = {<p>The human CRSP-Med coactivator complex is targeted by a diverse array of sequence-specific regulatory proteins. Using EM and single-particle reconstruction techniques, we recently completed a structural analysis of CRSP-Med bound to VP16 and SREBP-1a. Notably, these activators induced distinct conformational states upon binding the coactivator. Ostensibly, these different conformational states result from VP16 and SREBP-1a targeting distinct subunits in the CRSP-Med complex. To test this, we conducted a structural analysis of CRSP-Med bound to either thyroid hormone receptor (TR) or vitamin D receptor (VDR), both of which interact with the same subunit (Med220) of CRSP-Med. Structural comparison of TR- and VDR-bound complexes (at a resolution of 29 A) indeed reveals a shared conformational feature that is distinct from other known CRSP- Med structures. Importantly, this nuclear receptor-induced structural shift seems largely dependent on the movement of Med220 within the complex.</p>
},
	keywords = {Bacterial Proteins, Binding Sites, Calcitriol, Genetic, Hela Cells, Humans, Protein Binding, Protein Conformation, Receptors, Thyroid Hormone, Trans-Activators, Transcription},
	issn = {1545-9993},
	doi = {10.1073/pnas.1100640108},
	author = {Taatjes, Dylan J and Schneider-Poetsch, Tilman and Tjian, Robert}
}
