1G2N
CRYSTAL STRUCTURE OF THE LIGAND BINDING DOMAIN OF THE ULTRASPIRACLE PROTEIN USP, THE ORTHOLOG OF RXRS IN INSECTS
Summary for 1G2N
| Entry DOI | 10.2210/pdb1g2n/pdb |
| Descriptor | ULTRASPIRACLE PROTEIN, L-ALPHA-PHOSPHATIDYL-BETA-OLEOYL-GAMMA-PALMITOYL-PHOSPHATIDYLETHANOLAMINE (3 entities in total) |
| Functional Keywords | antiparallel alpha-helical sandwich, structural proteomics in europe, spine, structural genomics, gene regulation |
| Biological source | Heliothis virescens (tobacco budworm) |
| Total number of polymer chains | 1 |
| Total formula weight | 30672.65 |
| Authors | Billas, I.M.L.,Moulinier, L.,Rochel, N.,Moras, D.,Structural Proteomics in Europe (SPINE) (deposition date: 2000-10-20, release date: 2001-04-21, Last modification date: 2024-02-07) |
| Primary citation | Billas, I.M.,Moulinier, L.,Rochel, N.,Moras, D. Crystal structure of the ligand-binding domain of the ultraspiracle protein USP, the ortholog of retinoid X receptors in insects. J.Biol.Chem., 276:7465-7474, 2001 Cited by PubMed Abstract: The major postembryonic developmental events happening in insect life, including molting and metamorphosis, are regulated and coordinated temporally by pulses of ecdysone. The biological activity of this steroid hormone is mediated by two nuclear receptors: the ecdysone receptor (EcR) and the Ultraspiracle protein (USP). The crystal structure of the ligand-binding domain from the lepidopteran Heliothis virescens USP reported here shows that the loop connecting helices H1 and H3 precludes the canonical agonist conformation. The key residues that stabilize this unique loop conformation are strictly conserved within the lepidopteran USP family. The presence of an unexpected bound ligand that drives an unusual antagonist conformation confirms the induced-fit mechanism accompanying the ligand binding. The ligand-binding pocket exhibits a retinoid X receptor-like anchoring part near a conserved arginine, which could interact with a USP ligand functional group. The structure of this receptor provides the template for designing inhibitors, which could be utilized as a novel type of environmentally safe insecticides. PubMed: 11053444DOI: 10.1074/jbc.M008926200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.65 Å) |
Structure validation
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