Intracellular receptors

Under development!!! Signal recognition particle receptor Signal recognition particle receptor . Water molecules are shown as red spheres. . Receptor for activated C kinase 1 Receptor for activated protein kinase C 1 Nuclear receptors Nuclear receptors Thyroid hormone receptor The Retinoic acid receptor The . RA Mediated T-reg Differentiation; Retinoic acid acts as the ligand for the Retinoic Acid Receptor-α (RARα) / Retinoid X Receptor-α (RXRα) heterodimer (PDB entry 1dkf). The Ligand binding domain for each piece of the dimer has a nearly identical structure of an . 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 and the . When RARα/RXRα proteins form a heterodimer, the overall structure of the larger dimer is comparable to that of an RXRα homodimer, likely due to the many similarities these two molecules share. RARα and RXRα rely on residues from the H7, H8, H9, H10, L8-9, and L9-10 domains of both molecules to form the . The sequence identity between the two molecules on the dimer interface is 0.33, demonstrating that 33% of the interacting residues are homologous between the different proteins. The residues of α that are interacting in the heterodimer are as follows: Hydrophobic residues: L356, F374, P375, L378, M379, I381 and A389 (yellow); Negatively charged residues: D338, D349, E353, E357, D383, and E393 (red); Positively charged residues: K360, R364, H372, K376, K380, and R385 (blue); Hydrophilic residues: Q315, Q352, T382, and S386 (green). The residues of α that are interacting in the heterodimer are as follows: Hydrophobic residues: Y402, P417, F420, A421, L424, L425, L427, P428, A429, and L435 (yellow); Negatively charged residues: E357, D384, E395, E399, E406, and E439 (red); Positively charged residues: R353, K361, R398, K410, K422, R426, R431, and K436 (blue); Hydrophilic residues: S432 (green). PPAR-gamma Pioglitazone is a selective agonist for Peroxisome Proliferator-Activated Receptor Gamma Liver X receptor Bile acid receptor Vitamin D receptor Pregnane X receptor Retinoid X receptor Estrogen receptor Ivan Koutsopatriy estrogen receptor Estrogen receptor#Structure of estradiol metal chelate and estrogen receptor complex: The basis for designing a new class of SERMs Estrogen receptor#Estrogen receptor α complexed with raloxifene and a corepressor peptide Tamoxifen and the Estrogen receptor Student Project 10 for UMass Chemistry 423 Spring 2015 Estrogen-related receptor Glucocorticoid receptor Mineralocorticoid receptor Progesterone receptor Androgen receptor Liver receptor homolog-1? Endoplasmic reticulum/Sarcoplasmic reticulum receptors Ligand-gated Calcium channels Ryanodine receptor SEE ALSO: Hormones and their receptors Hormone Receptor

spinqualitylabelsall models Human androgen receptor ligand-binding domain complex with modulator (PDB code 3b5r) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image