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Eur Biophys J. 2010 Oct;39(11):1471-5. doi: 10.1007/s00249-010-0602-2. Epub 2010 Apr 3.

A canonical cation-π interaction stabilizes the agonist conformation of estrogen-like nuclear receptors.

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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.


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.

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