Article
Role of residues 143 and 278 of the human nuclear Vitamin D receptor in the full-length and Delta165-215 deletion mutant.
The Journal of steroid biochemistry and molecular biology - 1 May 2004
Acevedo Alejandra, Stoynova Ludmilla, Davis Karen, Solórzano Ramona, Collins Elaine D
Abstract excerpt
Most of the actions of 1,25-dihydroxyvitamin D(3) [1,25(OH)(2)D(3)] are mediated by binding to the Vitamin D nuclear receptor (VDR). The crystal structure of a deletion mutant (Delta165-215) of the VDR ligand-binding domain (LBD) bound to 1,25(OH)(2)D(3) indicates that amino acid residues tyrosine-143 and serine-278 form hydrogen bonding interactions with the 3-hydroxyl group of 1,25(OH)(2)D(3). Studies of VDR...
Topics
- Animals
- Base Sequence
- COS Cells
- DNA Primers
- Humans
- Ligands
- Mutation
- Protein Binding
- Receptors, Calcitriol
- Sequence Deletion
