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| A canonical structure for the ligand-binding domain of nuclear receptors |
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| Author(s): Wurtz JM, Bourguet W, Renaud JP, Vivat V, Chambon P, Moras D, Gronemeyer H |
| Source: NATURE STRUCTURAL BIOLOGY Volume: 3 Issue: 1 Pages: 87-94 Published: JAN 1996 |
| Times Cited: 562 References: 51 |
| Abstract: The ability of nuclear receptors (NRs) to activate transcription of target genes requires the binding of cognate ligands to their ligand-binding domains (LBDs). Information provided by the three-dimensional structures of the unliganded RXR alpha and the liganded RAR gamma LBDs has been incorporated into a general alignment of the LBDs of all NRs. A twenty amino-acid region constitutes a NR-specific signature and contains most of the conserved residues that stabilize the core of the canonical fold of NR LBDs. A common ligand-binding pocket, involving predominantly hydrophobic residues, is inferred by homology modelling of the human RXR alpha and glucocorticoid receptor ligand-binding sites according to the RAR gamma holo-LBD structure. Mutant studies support these models, as well as a general mechanism for ligand-induced activation deduced from the comparison of the transcriptionally active RAR gamma holo- and inactive RXR alpha apo-LBD structures. |
| Document Type: Article |
| Language: English |
Addresses:
1. UNIV STRASBOURG 1, CU STRASBOURG, COLL FRANCE, INST GENET & BIOL MOLEC & CELLULAIRE, CNRS, INSERM, F-67404 ILLKIRCH GRAFFENSTADEN, FRANCE |
| Publisher: NATURE PUBLISHING CO, 345 PARK AVE SOUTH, NEW YORK, NY 10010-1707 |
| Subject Category: Biochemistry & Molecular Biology; Biophysics; Cell Biology |
| IDS Number: TN527 |
| ISSN: 1072-8368 |
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| | | | | | | | | Record from Web of Science® | | | | | | | | | |