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• W2029679505 endingPage "1013" @default.
• W2029679505 startingPage "1008" @default.
• W2029679505 abstract "Nuclear hormone receptors (NRs) are potential targets for therapeutic approaches to many clinical conditions, including cancer, diabetes, and neurological diseases. The crystal structure of the ligand binding domain of agonist-bound NRs enables the design of compounds with agonist activity. However, with the exception of the human estrogen receptor-alpha, the lack of antagonist-bound inactive receptor structures hinders the rational design of receptor antagonists. In this study, we present a strategy for designing such antagonists. We constructed a model of the inactive conformation of human retinoic acid receptor-alpha by using information derived from antagonist-bound estrogen receptor-alpha and applied a computer-based virtual screening algorithm to identify retinoic acid receptor antagonists. Thus, the currently available crystal structures of NRs may be used for the rational design of antagonists, which could lead to the development of novel drugs for a variety of diseases." @default.
• W2029679505 created "2016-06-24" @default.
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• W2029679505 date "2000-02-01" @default.
• W2029679505 modified "2023-10-07" @default.
• W2029679505 title "Rational discovery of novel nuclear hormone receptor antagonists" @default.
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• W2029679505 doi "https://doi.org/10.1073/pnas.97.3.1008" @default.
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