2HC4: Crystal Structure Of The Lbd Of Vdr Of Danio Rerio In Complex With Calcitriol

The crystal structure of the ligand binding domain (LBD) of the wild-type Vitamin D receptor (VDR) of zebrafish bound to Gemini, a synthetic agonist ligand with two identical side chains branching at carbon 20 reveals a ligand-dependent structural rearrangement of the ligand binding pocket (LBP). The rotation of a Leu side chain opens the access to a channel that can accommodate the second side chain of the ligand. The 25% increase of the LBP's volume does not alter the essential agonist features of VDR. The possibility to adapt the LBP to novel ligands with different chemistry and/or structure opens new perspectives in the design of more specifically targeted ligands.
PDB ID: 2HC4Download
MMDB ID: 45466
PDB Deposition Date: 2006/6/15
Updated in MMDB: 2007/10
Experimental Method:
x-ray diffraction
Resolution: 2.2  Å
Source Organism:
synthetic construct
Similar Structures:
Biological Unit for 2HC4: dimeric; determined by author and by software (PISA)
Molecular Components in 2HC4
Label Count Molecule
Proteins (2 molecules)
Vitamin D Receptor(Gene symbol: vdra)
Molecule annotation
Src-1 From Nuclear Receptor Coactivator 1(Gene symbol: NCOA1)
Molecule annotation
Chemical (1 molecule)
* Click molecule labels to explore molecular sequence information.

Citing MMDB