Structural investigation of the ligand binding domain of the zebrafish VDR in complexes with 1alpha,25(OH)2D3 and Gemini: purification, crystallization and preliminary X-ray diffraction analysis

Fabrice Ciesielski (1) , Natacha Rochel (1) , André Mitschler (1) , Alexander Kouzmenko (2) , Dino Moras (1)

1 IGBMC - Institut de génétique et biologie moléculaire et cellulaire
2 UTokyo - The University of Tokyo

The nuclear receptor of Vitamin D can be activated by a large number of agonist molecules with a wide spectrum in their stereochemical framework. Up to now most of our structural information related to the protein-ligand complex formation is based on an engineered ligand binding domain (LBD) of the human receptor. We now have extended our database, using a wild-type LBD from zebrafish that confirms the previously reported results and allows to investigate the binding of ligands that induce significant conformational changes at the protein level.

Domaines: Biochimie, Biologie Moléculaire

Fabrice Ciesielski, Natacha Rochel, André Mitschler, Alexander Kouzmenko, Dino Moras. Structural investigation of the ligand binding domain of the zebrafish VDR in complexes with 1alpha,25(OH)2D3 and Gemini: purification, crystallization and preliminary X-ray diffraction analysis. Journal of Steroid Biochemistry and Molecular Biology, 2004, 89-90 (1-5), pp.55-59. ⟨10.1016/j.jsbmb.2004.03.109⟩. ⟨hal-04138418⟩