ISDA: 3AUN

Deposition Date 2011-02-10

Release Date 2012-02-15

Last Version Date 2023-11-01

Entry Detail

PDB ID:

3AUN

Keywords:

TRANSCRIPTION

Title:

Crystal structure of the rat vitamin D receptor ligand binding domain complexed with YR335 and a synthetic peptide containing the NR2 box of DRIP 205

Biological Source:

Source Organism(s):

Rattus norvegicus (Taxon ID: 10116)
synthetic construct (Taxon ID: 32630)

Expression System(s):

Escherichia coli

Method Details:

Experimental Method:

X-RAY DIFFRACTION

Resolution:

1.81 Å

R-Value Free:

0.23

R-Value Work:

0.19

R-Value Observed:

0.19

Space Group:

P 21 21 2

Download Validation Report

Macromolecular Entities

Structures with similar UniProt ID

Protein Blast

Polymer Type:polypeptide(L)
Molecule:Vitamin D3 receptor
Gene (Uniprot):Vdr
Mutagens:DEL(165-211) mutant
Chain IDs:A
Chain Length:265
Number of Molecules:1
Biological Source:Rattus norvegicus

UniProt ID:P13053 Pfam ID:PF00104

Structures with similar UniProt ID

Protein Blast

Polymer Type:polypeptide(L)
Molecule:DRIP 205 NR2 box peptide
Gene (Uniprot):MED1
Chain IDs:B
Chain Length:13
Number of Molecules:1
Biological Source:synthetic construct

UniProt ID:Q15648

Ligand Molecules

YR4

Primary Citation

Design, synthesis and X-ray crystallographic study of new nonsecosteroidal vitamin D receptor ligands

Demizu, Y, Takahashi, T, Kaneko, F, Sato, Y, Okuda, H, Ochiai, E, Horie, K, Takagi, K, Kakuda, S, Takimoto-Kamimura, M, Kurihara, M.Show

Bioorg. Med. Chem. Lett. 21 6104 6107 (2011)

PMID: 21889334 DOI: 10.1016/j.bmcl.2011.08.047

Abstact

We designed and synthesized nonsecosteroidal vitamin D receptor (VDR) ligands that formed H-bonds with six amino acid residues (Tyr143, Ser233, Arg270, Ser274, His301 and His393) of the VDR ligand-binding domain. The ligand YR335 exhibited potent transcriptional activity, which was comparable to those of 1α,25-dihydroxyvitamin D(3) and YR301. The crystal structure of the complex formed between YR335 and the VDR ligand-binding domain was solved, which revealed that YR335 formed H-bonds with the six amino acid residues mentioned above.

Legend

Protein

Chemical

Disease

Primary Citation of related structures

Abstact

Feedback Form