Fiche publication
Date publication
janvier 2012
Auteurs
Membres identifiés du Cancéropôle Est :
Dr MORAS Dino
,
Dr ROCHEL-GUIBERTEAU Natacha
,
Dr OSZ-PAPAI Judit
Tous les auteurs :
Osz J, Pethoukhov MV, Sirigu S, Svergun DI, Moras D, Rochel N
Lien Pubmed
Résumé
PPARgamma is a key regulator of glucose homeostasis and insulin sensitization. PPARgamma must heterodimerize with its dimeric partner, the retinoid X receptor (RXR), to bind DNA and associated coactivators such as p160 family members or PGC-1alpha to regulate gene networks. To understand how coactivators are recognized by the functional heterodimer PPARgamma/RXRalpha and to determine the topological organization of the complexes, we performed a structural study using small angle X-ray scattering of PPARgamma/RXRalpha in complex with DNA from regulated gene and the TIF2 receptor interacting domain (RID). The solution structures reveal an asymmetry of the overall structure due to the crucial role of the DNA in positioning the heterodimer and indicate asymmetrical binding of TIF2 to the heterodimer.
Référence
PPAR Res. 2012;2012:701412
