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• W2065291224 abstract "The crystal structure of the ligand binding domain (LBD) of the wild-type Vitamin D receptor (VDR) of zebrafish bound to Gemini, a synthetic agonist ligand with two identical side chains branching at carbon 20 reveals a ligand-dependent structural rearrangement of the ligand binding pocket (LBP). The rotation of a Leu side chain opens the access to a channel that can accommodate the second side chain of the ligand. The 25% increase of the LBP's volume does not alter the essential agonist features of VDR. The possibility to adapt the LBP to novel ligands with different chemistry and/or structure opens new perspectives in the design of more specifically targeted ligands." @default.
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• W2065291224 date "2007-03-01" @default.
• W2065291224 modified "2023-10-12" @default.
• W2065291224 title "Adaptability of the Vitamin D nuclear receptor to the synthetic ligand Gemini: Remodelling the LBP with one side chain rotation" @default.
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• W2065291224 doi "https://doi.org/10.1016/j.jsbmb.2006.12.003" @default.
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