VDR, DNA-binding domain (IPR042153)

Short name: DBD_VDR

Overlapping homologous superfamilies

Domain relationships


This entry represents the DNA-binding domain of vitamin D receptors (VDR). It is composed of two C4-type zinc fingers. Each zinc finger contains a group of four Cys residues which coordinates a single zinc atom. VDR interacts with a VDR response element, a direct repeat of GGTTCA DNA site with 3 bp spacer upstream of the target gene, and modulates the rate of transcriptional initiation [PMID: 11980721].

VDR is a member of the nuclear receptor (NR) superfamily that functions as classical endocrine receptors. VDR controls a wide range of biological activities including calcium metabolism, cell proliferation and differentiation, and immunomodulation. VDR is a high-affinity receptor for the biologically most active Vitamin D metabolite, 1alpha,25-dihydroxyvitamin D3 (1alpha,25(OH)2D3) [PMID: 1289951]. The binding of the ligand to the receptor induces a conformational change of the ligand binding domain (LBD) with consequent dissociation of corepressors. Upon ligand binding, VDR forms a heterodimer with the retinoid X receptor (RXR) that binds to vitamin D response elements (VDREs), recruits coactivators. This leads to the expression of a large number of genes. Approximately 200 human genes are considered to be primary targets of VDR and even more genes are regulated indirectly [PMID: 16848738]. Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, VDR has a central well conserved DNA binding domain (DBD) [PMID: 15242339], a variable N-terminal domain, a flexible hinge and a C-terminal ligand binding domain (LBD) [PMID: 10892345, PMID: 15520817].

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0043565 sequence-specific DNA binding

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.