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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



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



Journal of Biological Chemistry 279(47): 49330-7



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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Accession: 012062532

Download citation: RISBibTeXText

PMID: 15337744

DOI: 10.1074/jbc.m407999200


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