1DB1

CRYSTAL STRUCTURE OF THE NUCLEAR RECEPTOR FOR VITAMIN D COMPLEXED TO VITAMIN D

Summary for 1DB1

• Entry DOI: 10.2210/pdb1db1/pdb
• Descriptor: VITAMIN D NUCLEAR RECEPTOR, 5-{2-[1-(5-HYDROXY-1,5-DIMETHYL-HEXYL)-7A-METHYL-OCTAHYDRO-INDEN-4-YLIDENE]-ETHYLIDENE}-4-METHYLENE-CYCLOHEXANE-1,3-DIOL (3 entities in total)
• Functional Keywords: complex, gene regulation
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus: P11473
• Total number of polymer chains: 1
• Total formula weight: 29808.51

Authors

Rochel, N.,Wurtz, J.M.,Mitschler, A.,Klaholz, B.,Moras, D. (deposition date: 1999-11-02, release date: 2000-01-31, Last modification date: 2024-02-07)

Primary citation

Rochel, N.,Wurtz, J.M.,Mitschler, A.,Klaholz, B.,Moras, D.
The crystal structure of the nuclear receptor for vitamin D bound to its natural ligand.
Mol.Cell, 5:173-179, 2000

PubMed Abstract: 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.

PubMed: 10678179
DOI: 10.1016/S1097-2765(00)80413-X

Experimental method

X-RAY DIFFRACTION (1.8 Å)