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

J Steroid Biochem Mol Biol. 2004 May;89-90(1-5):55-9. doi: 10.1016/j.jsbmb.2004.03.109.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Calcitriol / metabolism*
  • Crystallography, X-Ray
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Conformation
  • Receptors, Calcitriol / chemistry*
  • Receptors, Calcitriol / isolation & purification
  • Receptors, Calcitriol / metabolism
  • Sequence Homology, Amino Acid
  • Zebrafish

Substances

  • Receptors, Calcitriol
  • Calcitriol