5YSY

Crystal structure of the human vitamin D receptor ligand binding domain complexed with (1R,2R,3R)-5-[(E)-2-{(1R,3aS,7aR)-1-[(R)-6-hydroxy-6-methylheptan-2-yl]-7a-methyl-2,3,3a,6,7,7a-hexahydro-1H-inden-4-yl}vinyl]-2-(3-hydroxypropyl)cyclohex-4-ene-1,3-diol

Summary for 5YSY

• Entry DOI: 10.2210/pdb5ysy/pdb
• Descriptor: Vitamin D3 receptor, (1R,2R,3R)-5-[(E)-2-[(1R,3aS,7aR)-7a-methyl-1-[(2R)-6-methyl-6-oxidanyl-heptan-2-yl]-1,2,3,3a,6,7-hexahydroinden-4-yl]e thenyl]-2-(3-oxidanylpropyl)cyclohex-4-ene-1,3-diol (3 entities in total)
• Functional Keywords: active ligand, complex, transcription
• Biological source: Homo sapiens (Human); More
• Cellular location: Nucleus : P11473
• Total number of polymer chains: 1
• Total formula weight: 29409.11

Authors

Takimoto-Kamimura, M.,Kakuda, S. (deposition date: 2017-11-16, release date: 2018-04-11, Last modification date: 2023-11-22)

Primary citation

Sawada, D.,Kakuda, S.,Takeuchi, A.,Kawagoe, F.,Takimoto-Kamimura, M.,Kittaka, A.
Effects of 2-substitution on 14-epi-19-nortachysterol-mediated biological events: based on synthesis and X-ray co-crystallographic analysis with the human vitamin D receptor.
Org. Biomol. Chem., 16:2448-2455, 2018

PubMed Abstract: Both 2α- and 2β-hydroxypropyl substituted 14-epi-1α,25-dihydroxy-19-nortachysterols were synthesized to study the human vitamin D receptor (hVDR) binding affinity, binding configurations, and interactions with amino acid residues in the ligand binding domain of hVDR by X-ray co-crystallographic analysis. In conjunction with our previous results on 14-epi-19-nortachysterol, 2-methylidene-, 2α-methyl-, 2β-methyl, and 2α-hydroxypropoxy-14-epi-19-nortachysterol, we propose a variety of effects of substitution at the C2 position in the 14-epi-19-nortachysterol skeleton on biological activities.

PubMed: 29560490
DOI: 10.1039/C8OB00158H

Experimental method

X-RAY DIFFRACTION (2 Å)