The RXR-alpha C-terminus T462 is a NMR sensor for coactivator peptide binding

Simple item page
dc.contributor.authorLu, Jianyunen_US
dc.contributor.authorChen, Mingheen_US
dc.contributor.authorDeKoster, Gregory T.en_US
dc.contributor.authorCistola, Daviden_US
dc.contributor.authorLi, Ellenen_US
dc.date.accessioned2011-04-15T16:38:52Zen_US
dc.date.accessioned2011-05-17T01:27:00Z
dc.date.available2011-04-15T16:38:52Zen_US
dc.date.available2011-05-17T01:27:00Z
dc.date.issued2008-02-22en_US
dc.description.abstractThe C-terminal activation function-2 (AF-2) helix plays a crucial role in retinoid X receptor alpha (RXRα)-mediated gene expression. Here, we report a nuclear magnetic resonance (NMR) study of the RXRα ligand-binding domain complexed with 9-cis-retinoic acid and a glucocorticoid receptorinteracting protein 1 peptide. The AF-2 helix and most of the C-terminal residues were undetectable due to a severe line-broadening effect. Due to its outstanding signal-to-noise ratio, the C-terminus residue, threonine 462 (T462) exhibited two distinct crosspeaks during peptide titration, suggesting that peptide binding was in a slow exchange regime on the chemical shift timescale. Consistently, the Kd derived from T462 intensity decay agreed with that derived from isothermal titration calorimetry. Furthermore, the exchange contribution to the 15N transverse relaxation rate was measurable in either T462 or the bound peptide. These results suggest that T462 is a sensor for coactivator binding and is a potential probe for AF-2 helix mobility. Originally published Biochemical and Biophysical Research Communications, Vol. 366, No. 4, Feb 2008en_US
dc.identifier.citationBiochemical and Biophysical Research Communications; 366:4 p. 932-937en_US
dc.identifier.pmidPMC2277333en_US
dc.identifier.urihttp://hdl.handle.net/10342/3341en_US
dc.language.isoen_USen_US
dc.publisherEast Carolina Universityen_US
dc.relation.urihttp://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6WBK-4RFC7NB-1&_user=10&_coverDate=02%2F22%2F2008&_rdoc=1&_fmt=high&_orig=gateway&_origin=gateway&_sort=d&_docanchor=&view=c&_acct=C000050221&_version=1&_urlVersion=0&_userid=10&md5=9b59a60c2a75fab67b2da162e745b283&searchtype=aen_US
dc.rightsAuthor notified of opt-out rights by Cammie Jennings prior to upload of this article.en_US
dc.subjectRXR alphaen_US
dc.subjectActivationen_US
dc.subjectGRIP1en_US
dc.subjectCoactivatoren_US
dc.subjectNMRen_US
dc.subjectIsothermal titration calorimetryen_US
dc.titleThe RXR-alpha C-terminus T462 is a NMR sensor for coactivator peptide bindingen_US
dc.typeArticleen_US

Files

Original bundle
Now showing 1 - 1 of 1
Thumbnail Image
Name:
RXR C terminus.pdf
Size:
929.27 KB
Format:
Adobe Portable Document Format
Download

Collections

Biochemistry and Molecular Biology