3AUN

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

Summary for 3AUN

• Entry DOI: 10.2210/pdb3aun/pdb
• Related: 2ZFX
• Descriptor: Vitamin D3 receptor, DRIP 205 NR2 box peptide, (2R)-2-{4-[3-(4-{[(2R)-2-hydroxy-3,3-dimethylbutyl]oxy}-3-methylphenyl)pentan-3-yl]-2-methylphenoxy}butane-1,4-diol, ... (4 entities in total)
• Functional Keywords: binding sites, biphenyl compounds, protein binding, tertiary, rats, receptors, calcitriol, vitamin d, transcription
• Biological source: Rattus norvegicus (rat); More
• Cellular location: Nucleus: P13053 Q15648
• Total number of polymer chains: 2
• Total formula weight: 32099.05

Authors

Kakuda, S.,Takimoto-Kamimura, M. (deposition date: 2011-02-10, release date: 2012-02-15, Last modification date: 2023-11-01)

Primary citation

Demizu, Y.,Takahashi, T.,Kaneko, F.,Sato, Y.,Okuda, H.,Ochiai, E.,Horie, K.,Takagi, K.,Kakuda, S.,Takimoto-Kamimura, M.,Kurihara, M.
Design, synthesis and X-ray crystallographic study of new nonsecosteroidal vitamin D receptor ligands
Bioorg.Med.Chem.Lett., 21:6104-6107, 2011

PubMed Abstract: 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.

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

Experimental method

X-RAY DIFFRACTION (1.81 Å)