Display Settings:


Send to:

Choose Destination
See comment in PubMed Commons below
Drug Discov Today. 2013 Jun;18(11-12):574-81. doi: 10.1016/j.drudis.2013.01.001. Epub 2013 Jan 5.

3D structures and ligand specificities of nuclear xenobiotic receptors CAR, PXR and VDR.

Author information

  • 1Division of Pharmaceutics, College of Pharmacy, Jinan University, 601 Huangpu Avenue West, Guangzhou, Guangdong 510632, China. bj.wu@hotmail.com


The nuclear receptors constitutive androstane receptor (CAR), pregnane X receptor (PXR) and vitamin D receptor (VDR) control a large array of genes that code for important proteins in humans including metabolic enzymes and transporters. 3D structures for the ligand-binding domain (LBD) of these receptors are abundantly available, providing valuable insights into the ligand-binding specificity as well as the activation mechanisms. The ligand-binding site of PXR is large and flexible, whereas those of CAR and VDR are compact and rigid, respectively. In general, the ligand profiles of the receptors are in agreement with the LBD structures. The crystal structures have greatly helped us to understand the promiscuity and/or specificity of CAR, PXR and VDR.

Copyright © 2013 Elsevier Ltd. All rights reserved.

[PubMed - indexed for MEDLINE]
PubMed Commons home

PubMed Commons

How to join PubMed Commons

    Supplemental Content

    Icon for Elsevier Science
    Loading ...
    Write to the Help Desk