Summary
PDB 1DB1 deposited: 1999-11-02 modified: 2009-02-24
Title CRYSTAL STRUCTURE OF THE NUCLEAR RECEPTOR FOR VITAMIN D COMPLEXED TO VITAMIN D
Authors Klaholz, B., Mitschler, A., Moras, D., Rochel, N., Wurtz, J.M.
Method X-RAY DIFFRACTION
Structure factors resolution 1.8 rfactor 0.191 rfree 0.214
DPI 0.29 theoretical min: 0.13
Citations

The action of 1 alpha, 25-dihydroxyvitamin D3 is mediated by its nuclear receptor (VDR), a ligand-dependent transcription regulator. We report the 1.8 A resolution crystal structure of the complex between a VDR ligand-binding domain (LBD) construct lacking the highly variable VDR-specific insertion domain and vitamin D. The construct exhibits the same binding affinity for vitamin D and transactivation ability as the wild-type protein, showing that the N-terminal part of the LBD is essential for its structural and functional integrity while the large insertion peptide is dispensable. The structure reveals the active conformation of the bound ligand and allows understanding of the different binding properties of some synthetic analogs.

Mol Cell. 2000 Jan;5(1):173-9.

Cross References
Database source Identifier Description
PubMed 10678179 MOCEFL
Biomolecule Structure Assembly Serial Assembly Type Conformational State Chains Ligands Atoms
1DB1/0 1DB1 0 monomer 0 1 1 1996