Calcitriol receptor

1DB1, 1IE8, 1IE9, 1KB2, 1KB4, 1KB6, 1S0Z, 1S19, 1TXI, 1YNW, 2HAM, 2HAR, 2HAS, 2HB7, 2HB8, 3A2I, 3A2J, 3A3Z, 3A40, 3A78, 3AUQ, 3AUR, 3AX8, 3AZ1, 3AZ2, 3AZ3, 3B0T, 3CS4, 3CS6, 3KPZ, 3M7R, 3OGT, 3P8X, 3TKC, 3VHW, 4G2I, 3W0A, 3W0C, 3W0Y, 3WGP, 3WWR, 4ITE, 4ITF, 4PA2, 3X31, 3X36742122337ENSG00000111424ENSMUSG00000022479P11473P48281NM_000376NM_001017535NM_001017536NM_001364085NM_009504NP_000367NP_001017535NP_001017536NP_001351014NP_033530The calcitriol receptor, more commonly known as the vitamin D receptor (VDR) and also known as NR1I1 (nuclear receptor subfamily 1, group I, member 1), is a member of the nuclear receptor family of transcription factors. Calcitriol, the active form of vitamin D, binds to the VDR, which then forms a heterodimer with the retinoid-X receptor. This then binds to hormone response elements on DNA resulting in expression or transrepression of specific gene products. The VDR not only regulates transcriptional responses but also involved in microRNA-directed post transcriptional mechanisms. In humans, the vitamin D receptor is encoded by the VDR gene.2hb8: Crystal structure of VDR LBD in complex with 2alpha-methyl calcitriol1ynw: Crystal Structure of Vitmain D Receptor and 9-cis Retinoic Acid Receptor DNA-Binding Domains Bound to a DR3 Response Element1kb2: Crystal Structure of VDR DNA-binding Domain Bound to Mouse Osteopontin (SPP) Response Element1db1: CRYSTAL STRUCTURE OF THE NUCLEAR RECEPTOR FOR VITAMIN D COMPLEXED TO VITAMIN D1s0z: Crystal structure of the VDR LBD complexed to seocalcitol.2ham: Crystal structure of VDR LBD complexed to 2alpha-propyl-calcitriol2har: Crystal structure of VDR LBD in complex with 2 alpha-(3-hydroxy-1-propoxy) calcitriol1kb6: Crystal Structure of VDR DNA-binding Domain Bound to Rat Osteocalcin (OC) Response Element1ie9: Crystal Structure Of The Nuclear Receptor For Vitamin D Ligand Binding Domain Bound to MC12881s19: Crystal structure of VDR ligand binding domain complexed to calcipotriol.2has: Crystal structure of VDR LBD in complex with 2alpha-(1-propoxy) calcitriol1ie8: Crystal Structure Of The Nuclear Receptor For Vitamin D Ligand Binding Domain Bound to KH10601txi: Crystal structure of the vdr ligand binding domain complexed to TX5222hb7: Crystal structure of VDR LBD in complex with 2alpha(3-hydroxy-1-propyl) calcitriol1kb4: Crystal Structure of VDR DNA-binding Domain Bound to a Canonical Direct Repeat with Three Base Pair Spacer (DR3) Response Element The calcitriol receptor, more commonly known as the vitamin D receptor (VDR) and also known as NR1I1 (nuclear receptor subfamily 1, group I, member 1), is a member of the nuclear receptor family of transcription factors. Calcitriol, the active form of vitamin D, binds to the VDR, which then forms a heterodimer with the retinoid-X receptor. This then binds to hormone response elements on DNA resulting in expression or transrepression of specific gene products. The VDR not only regulates transcriptional responses but also involved in microRNA-directed post transcriptional mechanisms. In humans, the vitamin D receptor is encoded by the VDR gene. Glucocorticoids are known to decrease expression of VDR, which is expressed in most tissues of the body and regulate intestinal transport of calcium, iron and other minerals. This gene encodes the nuclear hormone receptor for vitamin D3. This receptor also functions as a receptor for the secondary bile acid lithocholic acid. The receptor belongs to the family of trans-acting transcriptional regulatory factors and shows similarity of sequence to the steroid and thyroid hormone receptors. Downstream targets of this nuclear hormone receptor are involved principally in mineral metabolism though the receptor regulates a variety of other metabolic pathways, such as those involved in the immune response and cancer. Mutations in this gene are associated with type II vitamin D-resistant rickets. A single nucleotide polymorphism in the initiation codon results in an alternate translation start site three codons downstream. Alternative splicing results in multiple transcript variants encoding the same protein. The vitamin D receptor plays an important role in regulating the hair cycle. Loss of VDR is associated with hair loss in experimental animals.Experimental studies have shown that the unliganded VDR interacts with regulatory regions in cWnt (wnt signaling pathway) and sonic hedgehog target genes and is required for the induction of these pathways during the postnatal hair cycle.These studies have revealed novel actions of the unliganded VDR in regulating the post-morphogenic hair cycle. Calcitriol receptor has been shown to interact with Click on genes, proteins and metabolites below to link to respective articles. This article incorporates text from the United States National Library of Medicine, which is in the public domain.