7E2E
Crystal structure of the Estrogen-Related Receptor alpha (ERRalpha) ligand-binding domain (LBD) in complex with an agonist DS45500853 and a PGC-1alpha peptide
Summary for 7E2E
| Entry DOI | 10.2210/pdb7e2e/pdb |
| Descriptor | Steroid hormone receptor ERR1, Peroxisome proliferator-activated receptor gamma coactivator 1-alpha, 1-[4-(3-tert-butyl-4-oxidanyl-phenoxy)phenyl]ethanone, ... (5 entities in total) |
| Functional Keywords | nuclear receptor, complex, agonist, transcription |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 4 |
| Total formula weight | 57270.97 |
| Authors | Ito, S.,Shinozuka, T.,Kimura, T.,Izumi, M.,Wakabayashi, K. (deposition date: 2021-02-05, release date: 2021-06-30, Last modification date: 2023-11-29) |
| Primary citation | Shinozuka, T.,Ito, S.,Kimura, T.,Izumi, M.,Wakabayashi, K. Discovery of a Novel Class of ERR alpha Agonists. Acs Med.Chem.Lett., 12:817-821, 2021 Cited by PubMed Abstract: A novel class of estrogen-related receptor α (ERRα) agonists has been discovered. A structure-activity relationship study of high-throughput screening hits and led to the discovery of benzimidazole (DS20362725) and acetophenone analogue (DS45500853). The X-ray crystal structure of the ERRα ligand-binding domain in complex with and PGC-1α coactivator peptide revealed conformational changes in the ligand-binding pocket to accommodate and the key interaction between the protein and ligand. Since both analogues avoided PPARγ transcriptional activity, they can be useful tool compounds for investigating biological ERRα functions. PubMed: 34055231DOI: 10.1021/acsmedchemlett.1c00100 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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