Retinoid X receptor (RXR) serves as a promiscuous heterodimerization partner for many nuclear receptors through the identity box, a 40-amino acid subregion within the ligand binding domain (LBD). RXR partners include thyroid hormone receptors (TRs), retinoic acid receptors (RARs), peroxisome proliferator-activated receptor, several constitutive active orphan nuclear receptors (e.g. nuclear growth factor I-B), oxysterol receptors, and constitutive androstane receptors. RXRs also form homodimers to mediate the effects of 9-cis-retinoic acid (9-cRA). Depending on these protein-protein interactions, RXR-containing complexes have distinct ligand-dependent and constitutive functions. The LBD is functionally complex and mediates ligand binding, receptor homo- and heterodimerization, repression of transcription in the absence of ligand, and ligand-dependent activation of transcription. Hormone binding to the structurally conserved LBD of the RXR triggers a conformational change that principally affects the conserved C-terminal transactivation helix H12 involved in transcriptional activation. Coactivators directly recruited by liganded receptors include members of the steroid receptor coactivator/p160 family such as SRC-1, transcriptional intermediary factor 2/glucocorticoid receptor interacting protein 1, and RAC3/activator of thyroid and retinoic acid receptors/amplified in breast cancer 1.
forma física
Clear and colorless frozen liquid solution
Nota de preparo
Use a manual defrost freezer and avoid repeated freeze-thaw cycles. While working, please keep sample on ice.
Science (New York, N.Y.), 284(5413), 479-482 (1999-04-16)
The cytokines LIF (leukemia inhibitory factor) and BMP2 (bone morphogenetic protein-2) signal through different receptors and transcription factors, namely STATs (signal transducers and activators of transcription) and Smads. LIF and BMP2 were found to act in synergy on primary fetal
The nuclear receptor superfamily: the second decade.
D J Mangelsdorf et al.
Cell, 83(6), 835-839 (1995-12-15)
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