Intracellular receptors
From Proteopedia
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The <scene name='51/516466/Cv/4'>all-trans retinoid acid binds to the hydrophobic pocket of RARγ</scene>. | The <scene name='51/516466/Cv/4'>all-trans retinoid acid binds to the hydrophobic pocket of RARγ</scene>. | ||
*[[RA Mediated T-reg Differentiation]]; Retinoic acid acts as the ligand for the Retinoic Acid Receptor-α (RARα) / Retinoid X Receptor-α (RXRα) heterodimer | *[[RA Mediated T-reg Differentiation]]; Retinoic acid acts as the ligand for the Retinoic Acid Receptor-α (RARα) / Retinoid X Receptor-α (RXRα) heterodimer | ||
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| + | <scene name='51/519788/Cv/1'>RARα-RXRα interaction</scene> (PDB entry [[1dkf]]). | ||
| + | The Ligand binding domain for each piece of the dimer has a nearly identical structure of an <scene name='RA_Mediated_T-reg_Differentiaition/Alpha-helical_domains/2'>Tα-helical sandwich</scene>. These alpha helices form a total of 12 domains per protein (referred to as H1-12), with an additional 2 beta sheets as well. Additionally, the α-helical sandwich formed has been shown to bind All-Trans Retinoic Acid (ATRA), the isomer of RA used by the body. Both monomers contain two regions of activity, the <scene name='RA_Mediated_T-reg_Differentiaition/Dimerization_interface/3'>dimerization interface</scene> and the <scene name='RA_Mediated_T-reg_Differentiaition/Ligand_binding_pockets/1'> ligand binding pocket </scene>.<ref> PMID: 10882070 </ref> | ||
* [[PPAR-gamma]] | * [[PPAR-gamma]] | ||
* [[Pioglitazone]] is a selective agonist for Peroxisome Proliferator-Activated Receptor Gamma | * [[Pioglitazone]] is a selective agonist for Peroxisome Proliferator-Activated Receptor Gamma | ||
Revision as of 11:35, 19 May 2021
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References
- ↑ Bourguet W, Vivat V, Wurtz JM, Chambon P, Gronemeyer H, Moras D. Crystal structure of a heterodimeric complex of RAR and RXR ligand-binding domains. Mol Cell. 2000 Feb;5(2):289-98. PMID:10882070
- ↑ Li MJ, Greenblatt HM, Dym O, Albeck S, Pais A, Gunanathan C, Milstein D, Degani H, Sussman JL. Structure of estradiol metal chelate and estrogen receptor complex: The basis for designing a new class of selective estrogen receptor modulators. J Med Chem. 2011 Apr 7. PMID:21473635 doi:10.1021/jm200192y
