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1r20

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{{STRUCTURE_1r20| PDB=1r20 | SCENE= }}
{{STRUCTURE_1r20| PDB=1r20 | SCENE= }}
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'''Crystal structure of the ligand-binding domains of the heterodimer EcR/USP bound to the synthetic agonist BYI06830'''
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===Crystal structure of the ligand-binding domains of the heterodimer EcR/USP bound to the synthetic agonist BYI06830===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_14595375}}
==About this Structure==
==About this Structure==
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[[Category: Structural genomic]]
[[Category: Structural genomic]]
[[Category: Structural proteomics in europe]]
[[Category: Structural proteomics in europe]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Apr 13 08:10:26 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 08:05:33 2008''

Revision as of 05:05, 28 July 2008

Image:1r20.png

Template:STRUCTURE 1r20

Crystal structure of the ligand-binding domains of the heterodimer EcR/USP bound to the synthetic agonist BYI06830

Template:ABSTRACT PUBMED 14595375

About this Structure

1R20 is a Protein complex structure of sequences from Heliothis virescens. Full crystallographic information is available from OCA.

Reference

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

Page seeded by OCA on Mon Jul 28 08:05:33 2008

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