Evidence for ligand-independent transcriptional activation of the human estrogen-related receptor alpha (ERRalpha) : crystal structure of ERRalpha ligand binding domain in complex with peroxisome proliferator-activated receptor coactivator-1alpha
Kallen, J.; Schlaeppi, J-Marc.; Bitsch, F.; Filipuzzi, I.; Schilb, A.; Riou, V.; Graham, A.; Strauss, A.; Geiser, M.; Fournier, B.
Journal of Biological Chemistry 279(47): 49330-49337
The crystal structure of the ligand binding domain (LBD) of the estrogen-related receptor alpha(ERRalpha, NR3B1) complexed with a coactivator peptide from peroxisome proliferator-activated receptor coactivator-1alpha (PGC-1alpha) reveals a transcriptionally active conformation in the absence of a ligand. This is the first x-ray structure of ERRalpha LBD, solved to a resolution of 2.5 ANG, and the first structure of a PGC-1alpha complex.