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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

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Date 2004 Jul 1
PMID 15225747
Citations 15
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Abstract

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.

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