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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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A canonical structure for the ligand-binding domain of nuclear receptors.

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.[1]

References

  1. A canonical structure for the ligand-binding domain of nuclear receptors. Wurtz, J.M., Bourguet, W., Renaud, J.P., Vivat, V., Chambon, P., Moras, D., Gronemeyer, H. Nat. Struct. Biol. (1996) [Pubmed]
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