The DNA-binding domain of peroxisome proliferator-activated receptors (PPAR) like nuclear receptor family
The DNA-binding domain of peroxisome proliferator-activated receptors (PPAR) like nuclear receptor family is composed of two C4-type zinc fingers. Each zinc finger contains a group of four Cys residues which co-ordinates a single zinc atom. These domains interact with specific DNA sites upstream of the target gene and modulate the rate of transcriptional initiation. This family includes three known types of nuclear receptors: peroxisome proliferator-activated receptors (PPAR), REV-ERB receptors and Drosophila ecdysone-induced protein 78 (E78). Like other members of the nuclear receptor (NR) superfamily of ligand-activated transcription factors, PPAR-like receptors have a central well conserved DNA binding domain (DBD), a variable N-terminal domain, a non-conserved hinge and a C-terminal ligand binding domain (LBD).
Structure:3DZU_D; Zn binding site of human Rxr Alpha Nuclear Receptor Complex DNA binding domain, contacts determined at 3.5A - View structure with Cn3D
Comment:Zinc finger, C4-type: The domain contains two groups of four Cys residues. Each group is involved in the coordination of a single zinc atom.
Jiyao W et al.(2023). "The conserved domain database in 2023.",