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Vitamin D Receptor Home Page

Purpose and Program

Modifications and Mutagenesis

Homology

Interactions and Bibliography

Vitamin D Nuclear Receptor (VDR)

Please note this site is still under construction, and forgive us our appearance.

Ligand-binding Features Analyzed by Chemical Modification, Site-directed Mutagenisis and Homology-Extension Modeling

Rahul Ray, Narasimha Swamy
Wenrong Xu, George J. Maalouf
Scott C. Mohr


Image (ribbon) of VDR-LDB model

Model I

Please Note: This refined version of Model I was posted on 5/15/2000. It replaces the earlier version posted in October 1999.
View the PDB file in HTML
Download the PDB file

Model II

View the PDB file in HTML
Download the PDB file

INTRODUCTION

1,25-dihydroxyvitamin D3 [1,25-(OH)2-D3] or "vitamin D hormone" plays multiple roles in the regulation of animal metabolism. These are effected in two ways: (1) at the level of the plasma membrane (by a vitamin D membrane receptor) and (2) at the level of gene transcription. This web site is dedicated to information about the key protein involved in the second process.

Domain structure of VDR

VDR has a domain structure homologous to that of the other nuclear receptors (see next section). Its 427 amino acids encompass a short N-terminal activation-function 1 (AF-1) domain (A/B), a DNA-binding domain (DBD) containing two Zn2+-fingers (C), a flexible "hinge" region (D) that includes nuclear localization signals and an HSP-70 site, and finally the ligand-binding domain (LBD or "E") whose C-terminal end also has transcriptional activation function(s) (AF-2).

(bar diagram of VDR domains)
A/B C D E
The nuclear receptor (NR) superfamily
X-ray structures of ligand-binding domains (LBDs)



Sean Quinlan <wwwadmin@darwin.bu.edu>
last modified: Saturday, October 30, 1999 11:05:13 AM