1r1k

Crystal structure of the ligand-binding domains of the heterodimer EcR/USP bound to ponasterone A

spinqualitylabelsall models 1r1k, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1r1k is a 2 chain structure with sequence from Heliothis virescens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.9Å Ligands: EPH, P1A Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ECR_HELVI Receptor for ecdysone. Binds to ecdysone response elements (ECRES) (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The ecdysteroid hormones coordinate the major stages of insect development, notably moulting and metamorphosis, by binding to the ecdysone receptor (EcR); a ligand-inducible nuclear transcription factor. To bind either ligand or DNA, EcR must form a heterodimer with ultraspiracle (USP), the homologue of retinoid-X receptor. Here we report the crystal structures of the ligand-binding domains of the moth Heliothis virescens EcR-USP heterodimer in complex with the ecdysteroid ponasterone A and with a non-steroidal, lepidopteran-specific agonist BYI06830 used in agrochemical pest control. The two structures of EcR-USP emphasize the universality of heterodimerization as a general mechanism common to both vertebrates and invertebrates. Comparison of the EcR structures in complex with steroidal and non-steroidal ligands reveals radically different and only partially overlapping ligand-binding pockets that could not be predicted by molecular modelling and docking studies. These findings offer new perspectives for the design of insect-specific, environmentally safe insecticides. The concept of a ligand-dependent binding pocket in EcR provides an insight into the moulding of nuclear receptors to their ligand, and has potential applications for human nuclear receptors. Structural adaptability in the ligand-binding pocket of the ecdysone hormone receptor.,Billas IM, Iwema T, Garnier JM, Mitschler A, Rochel N, Moras D Nature. 2003 Nov 6;426(6962):91-6. Epub 2003 Nov 2. PMID:14595375 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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