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- W3127226292 abstract "Significance RORγt is a nuclear receptor associated with several diseases. Various synthetic ligands have been developed that target the canonical orthosteric or a second, allosteric pocket of RORγt. We show that orthosteric and allosteric ligands can simultaneously bind to RORγt and that their potency is positively influenced by the other ligand, a phenomenon called cooperative dual ligand binding. The mechanism behind cooperative binding in proteins is poorly understood, primarily due to the lack of structural data. We solved 12 crystal structures of RORγt, simultaneously bound to various orthosteric and allosteric ligands. In combination with molecular dynamics, we reveal a mechanism responsible for the cooperative binding behavior. Our comprehensive structural studies provide unique insights into how cooperative binding occurs in proteins." @default.
- W3127226292 created "2021-02-15" @default.
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- W3127226292 date "2021-02-03" @default.
- W3127226292 modified "2023-10-12" @default.
- W3127226292 title "Cooperativity between the orthosteric and allosteric ligand binding sites of RORγt" @default.
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- W3127226292 doi "https://doi.org/10.1073/pnas.2021287118" @default.
- W3127226292 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/8017705" @default.
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