title: A canonical cation-π interaction stabilizes the agonist conformation of estrogen-like nuclear receptors.
abstract: Representative crystal structures of the ligand-binding domain for the majority of nuclear receptors are currently available. A systematic comparative analysis of these structures identified an energetically favorable cation-π interaction that involves an amino acid located at the extreme C-terminal end and appears to form only in the agonist conformation of the estrogen receptor α, glucocorticoid, mineralocorticoid, progesterone, and androgen receptors. It is postulated that this cation-π interaction is used by members of the estrogen-like subfamily to provide additional stabilization to the transcriptional active conformation upon ligand binding.
authors.affiliation: Chemogenomics Laboratory, Research Program on Biomedical Informatics GRIB, Institut Municipal d'Investigació Mèdica and Universitat Pompeu Fabra, Parc de Recerca Biomèdica, Doctor Aiguader 88, 08003 Barcelona, Catalonia, Spain.
authors.forename: Núria
authors.initials: N
authors.lastname: Queralt-Rosinach
authors.forename: Jordi
authors.initials: J
authors.lastname: Mestres
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D019295:Computational Biology; D004967:Estrogens / Q000378:metabolism*; D006801:Humans; D008024:Ligands; D008958:Models, Molecular; D008969:Molecular Sequence Data; D055550:Protein Stability; D017434:Protein Structure, Tertiary; D051381:Rats; D018160:Receptors, Cytoplasmic and Nuclear / Q000819:agonists* / Q000737:chemistry* / Q000378:metabolism; D013816:Thermodynamics
chemical_list: D004967:Estrogens; D008024:Ligands; D018160:Receptors, Cytoplasmic and Nuclear