RXR alpha Activators

CD 3254 acts as a selective retinoid X receptor (RXR) alpha modulator, characterized by its unique structural features that promote specific ligand-receptor interactions. Its distinct conformation enhances the stability of RXR heterodimers, influencing gene transcription pathways. The compound exhibits unique reaction kinetics, facilitating rapid binding and dissociation rates, which may alter cellular responses. Additionally, its amphipathic nature allows for effective integration into lipid environments, modulating membrane fluidity and receptor accessibility.

9-cis-Retinoic acid, a retinoid, directly activates RXRα by binding to its ligand-binding domain. This leads to conformational changes that facilitate heterodimerization with other nuclear receptors, forming active transcriptional complexes that modulate gene expression.

Docosa-4Z,7Z,10Z,13Z,16Z,19Z-hexaenoic Acid functions as a potent modulator of RXR alpha, distinguished by its long-chain polyunsaturated structure that enables unique hydrophobic interactions with the receptor. This compound influences transcriptional activity through selective binding, promoting specific gene expression profiles. Its dynamic molecular behavior allows for versatile interactions within lipid bilayers, potentially affecting membrane dynamics and receptor localization, thereby modulating cellular signaling pathways.

LG100268, a synthetic retinoid, serves as a potent RXRα agonist. Its activation of RXRα involves binding to the ligand-binding domain, inducing a conformational change that promotes heterodimerization with other nuclear receptors and subsequent modulation of target gene expression.

Bexarotene, a rexinoid, directly activates RXRα by binding to its ligand-binding domain. This binding induces a conformational change in RXRα, enabling its heterodimerization with other nuclear receptors and facilitating the transcriptional regulation of target genes.

Bexarotene d4 acts as a selective RXR alpha agonist, characterized by its unique structural modifications that enhance binding affinity. This compound exhibits distinct conformational flexibility, allowing it to engage in specific hydrogen bonding and hydrophobic interactions with the receptor. Its kinetic profile suggests rapid association and dissociation rates, facilitating efficient modulation of gene transcription. Additionally, Bexarotene d4's lipophilic nature may influence membrane fluidity and receptor accessibility, impacting downstream signaling cascades.

SR11237, a selective RXR agonist, directly activates RXRα by binding to its ligand-binding domain. This binding triggers a conformational change that promotes heterodimerization with other nuclear receptors, initiating transcriptional cascades that modulate gene expression.

Cholecalciferol, also known as Vitamin D3, indirectly activates RXRα by modulating the vitamin D signaling pathway. Once converted to its active form, calcitriol, it forms a heterodimeric complex with RXRα, initiating transcriptional cascades that modulate gene expression.

AM580, a synthetic retinoid, directly activates RXRα by binding to its ligand-binding domain. This interaction induces a conformational change that facilitates heterodimerization with other nuclear receptors, initiating transcriptional programs that modulate gene expression.