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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

2004


ISSN/ISBN: 0021-9258
PMID: 15337744
DOI: 10.1074/jbc.m407999200
Accession: 012062532

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.

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