5H1E

Interaction between vitamin D receptor and coactivator peptide SRC2-3

Summary for 5H1E

• Entry DOI: 10.2210/pdb5h1e/pdb
• Descriptor: Vitamin D3 receptor, Nuclear receptor coactivator 2 peptide, 5-{2-[1-(5-HYDROXY-1,5-DIMETHYL-HEXYL)-7A-METHYL-OCTAHYDRO-INDEN-4-YLIDENE]-ETHYLIDENE}-4-METHYLENE-CYCLOHEXANE-1,3-DIOL, ... (4 entities in total)
• Functional Keywords: transcription, vitamin d3, vdre, rxr, co-factors, tif2
• Biological source: Rattus norvegicus (Rat); More
• Total number of polymer chains: 2
• Total formula weight: 32605.52

Authors

Egawa, D.,Itoh, T.,Kato, A.,Kataoka, S.,Anami, Y.,Yamamoto, K. (deposition date: 2016-10-08, release date: 2017-01-11, Last modification date: 2024-03-20)

Primary citation

Egawa, D.,Itoh, T.,Kato, A.,Kataoka, S.,Anami, Y.,Yamamoto, K.
SRC2-3 binds to vitamin D receptor with high sensitivity and strong affinity
Bioorg. Med. Chem., 25:568-574, 2017

PubMed Abstract: Vitamin D receptor (VDR) is a member of the nuclear receptor superfamily and regulates the expression of target genes through ligand binding. To express the target gene, coactivator binding to the VDR/ligand complex is essential. Although there are many coactivators in living cells, precise interactions between coactivators and VDR have not been clarified. Here, we synthesized two coactivator peptides, DRIP205-2 and SRC2-3, evaluated their affinity for the ligand-binding domain (LBD) of VDR using 1α,25-dihydroxyvitamin D, partial agonist 1, and antagonist 2 by surface plasmon resonance (SPR), and assessed their interaction modes with VDR-LBD using X-ray crystallographic analysis. This study showed that the SRC2-3 peptide is more sensitive to the ligands (agonist, partial agonist, and antagonist) and shows more intimate interactions with VDR-LBD than DRIP205-2 peptide.

PubMed: 27890450
DOI: 10.1016/j.bmc.2016.11.020

Experimental method

X-RAY DIFFRACTION (2.6 Å)