1N83
Crystal Structure of the complex between the Orphan Nuclear Hormone Receptor ROR(alpha)-LBD and Cholesterol
Summary for 1N83
| Entry DOI | 10.2210/pdb1n83/pdb |
| Descriptor | Nuclear receptor ROR-alpha, CHOLESTEROL (3 entities in total) |
| Functional Keywords | three-layered alpha helical sandwich, receptor, transcription regulation, nuclear protein, dna binding, lipid binding protein |
| Biological source | Homo sapiens (human) |
| Cellular location | Nucleus: P35398 |
| Total number of polymer chains | 1 |
| Total formula weight | 31900.93 |
| Authors | Kallen, J.A.,Schlaeppi, J.M.,Bitsch, F.,Geisse, S.,Geiser, M.,Delhon, I.,Fournier, B. (deposition date: 2002-11-19, release date: 2002-12-11, Last modification date: 2024-02-14) |
| Primary citation | Kallen, J.A.,Schlaeppi, J.M.,Bitsch, F.,Geisse, S.,Geiser, M.,Delhon, I.,Fournier, B. X-ray Structure of hROR(alpha) LBD at 1.63A: Structural and Functional data that Cholesterol or a Cholesterol derivative is the natural ligand of ROR(alpha) Structure, 10:1697-1702, 2002 Cited by PubMed Abstract: The retinoic acid-related orphan receptor alpha (RORalpha) is an orphan member of the subfamily 1 of nuclear hormone receptors. No X-ray structure of RORalpha has been described so far, and no ligand has been identified. We describe the first crystal structure of the ligand binding domain (LBD) of RORalpha, at 1.63 A resolution. This structure revealed a ligand present in the ligand binding pocket (LBP), which was identified by X-ray crystallography as cholest-5-en-3beta-ol (cholesterol). Moreover, RORalpha transcriptional activity could be modulated by changes in intracellular cholesterol level or mutation of residues involved in cholesterol binding. These findings suggest that RORalpha could play a key role in the regulation of cholesterol homeostasis and thus represents an important drug target in cholesterol-related diseases. PubMed: 12467577DOI: 10.1016/S0969-2126(02)00912-7 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.63 Å) |
Structure validation
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