Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1992524 | The Journal of Steroid Biochemistry and Molecular Biology | 2007 | 8 Pages |
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.
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Authors
Fabrice Ciesielski, Natacha Rochel, Dino Moras,