National Center for
3AUN: Crystal Structure Of The Rat Vitamin D Receptor Ligand Binding Domain Complexed With Yr335 And A Synthetic Peptide Containing The Nr2 Box Of Drip 205
Design, synthesis and X-ray crystallographic study of new nonsecosteroidal vitamin D receptor ligands
Bioorg. Med. Chem. Lett. (2011) 21 p.6104-6107
We designed and synthesized nonsecosteroidal vitamin D receptor (VDR) ligands that formed H-bonds with six amino acid residues (Tyr143, Ser233, Arg270, Ser274, His301 and His393) of the VDR ligand-binding domain. The ligand YR335 exhibited potent transcriptional activity, which was comparable to those of 1alpha,25-dihydroxyvitamin D(3) and YR301. The crystal structure of the complex formed between YR335 and the VDR ligand-binding domain was solved, which revealed that YR335 formed H-bonds with the six amino acid residues mentioned above.