© Boston University
Vitamin D Nuclear Receptor (VDR)(aka VDR.bu.edu)
PURPOSE & PROGRAM
Our aim is to provide an up-do-date, comprehensive resource dealing with the structure and function of the protein that mediates the gene-regulatory effects of vitamin D hormone (1,25-dihydroxyvitamin D3).
We present here homology-extension structural models of the ligand-binding domain (LBD) of the receptor protein. The models include bound ligands: 1,25-dihydroxyvitamin D3 itself; its hyperactive agonist analog, 20-epi-1,25-dihydroxyvitamin D3; and the newly discovered lactoneantagonist, "TEI-9647" [(23S)-25-dehydro-1a-hydroxyvitamin D3-26,23-lactone]. We also compile here the background information used to generate the models: mutation and modification data, the sequence/structure alignments and a bibliography. Additional related information and links to appropriate sites are included. Key features of the models are discussed and illustrated and downloadable PDB coordinates are furnished.
This website grows out of a collaboration between a bioinformatics subgroup led by Scott Mohr doing homology modeling in the BioMolecularEngineeringResearch-Center (BMERC) headed by Temple Smith in the College of Engineering at Boston University, and a vitamin D-oriented bioorganic chemistry and molecular biology laboratory headed by Rahul Ray at the Boston University School of Medicine. Inquiries relating to scientific content can be directed to firstname.lastname@example.org (S. Mohr) or email@example.com (R. Ray). The site has been created and is maintained by Sean Quinlan of BMERC (firstname.lastname@example.org).
We will maintain this site and make periodic updates so that it remains maximally useful to researchers and students with an interest in the genomic aspects of vitamin D function. Comments, corrections and suggestions are strongly encouraged.
Sean Quinlan <email@example.com> last modified: Saturday, October 30, 1999 11:05:05 AM