Retinoic acid receptor

spinqualitylabelsall models Structure of human retinoic acid receptorγ ligand-binding domain complex with all-trans retinoic acid (PDB entry 2lbd) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function Retinoic acid receptor (RAR) is a nuclear receptor activated by all-trans and 9-cis retinoic acid. RAR makes a heterodimer with retinoid X receptor (RXR). In the absence of ligand, the RAR/RXR complex binds the hormone response elements complexed with corepressor protein. Upon binding of the ligand, the corepressor disassociates from the receptor and associates with the coactivator leading to transcription activation. RAR contains a DNA-binding domain (DBD) and ligand-binding domain (LBD). There are 3 classes of RAR: α, β and γ. RARα plays an important role in mediating all-transretinoic acid signals. RARβ is a potent inhibitor of breast cancer cells in vitro. RARγ interacts with nuclear receptor co-repressor 1. See details of RAR/RXR complex in RA Mediated T-reg Differentiation. See also Intracellular receptors Relevance RARα is associated with tamoxifen resistance in breast cancer cells. RARβ is a prognostic indicator in stage I non-small-cell lung cancer. Disease RAR and RXR are important in a number of tumor cell models. Structural highlights The all-trans retinoid acid binds to the hydrophobic pocket of RARγ. 3D structures of retinoic acid receptor Retinoic acid receptor 3D structures

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