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1r20
From Proteopedia
(New page: 200px<br /><applet load="1r20" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r20, resolution 3.0Å" /> '''Crystal structure of ...) |
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| - | [[Image:1r20.gif|left|200px]]<br /><applet load="1r20" size=" | + | [[Image:1r20.gif|left|200px]]<br /><applet load="1r20" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1r20, resolution 3.0Å" /> | caption="1r20, resolution 3.0Å" /> | ||
'''Crystal structure of the ligand-binding domains of the heterodimer EcR/USP bound to the synthetic agonist BYI06830'''<br /> | '''Crystal structure of the ligand-binding domains of the heterodimer EcR/USP bound to the synthetic agonist BYI06830'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The ecdysteroid hormones coordinate the major stages of insect | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1R20 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Heliothis_virescens Heliothis virescens] with HWG and EPH as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1R20 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Heliothis_virescens Heliothis virescens] with <scene name='pdbligand=HWG:'>HWG</scene> and <scene name='pdbligand=EPH:'>EPH</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R20 OCA]. |
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[Category: Heliothis virescens]] | [[Category: Heliothis virescens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Billas, I | + | [[Category: Billas, I M.L.]] |
| - | [[Category: Garnier, J | + | [[Category: Garnier, J M.]] |
[[Category: Iwema, T.]] | [[Category: Iwema, T.]] | ||
[[Category: Mitschler, A.]] | [[Category: Mitschler, A.]] | ||
[[Category: Moras, D.]] | [[Category: Moras, D.]] | ||
[[Category: Rochel, N.]] | [[Category: Rochel, N.]] | ||
| - | [[Category: SPINE, Structural | + | [[Category: SPINE, Structural Proteomics in Europe.]] |
[[Category: EPH]] | [[Category: EPH]] | ||
[[Category: HWG]] | [[Category: HWG]] | ||
| Line 29: | Line 29: | ||
[[Category: structural proteomics in europe]] | [[Category: structural proteomics in europe]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:46:09 2008'' |
Revision as of 12:46, 21 February 2008
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Crystal structure of the ligand-binding domains of the heterodimer EcR/USP bound to the synthetic agonist BYI06830
Overview
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.
About this Structure
1R20 is a Protein complex structure of sequences from Heliothis virescens with and as ligands. 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 Thu Feb 21 14:46:09 2008
Categories: Heliothis virescens | Protein complex | Billas, I M.L. | Garnier, J M. | Iwema, T. | Mitschler, A. | Moras, D. | Rochel, N. | SPINE, Structural Proteomics in Europe. | EPH | HWG | Alpha-helical sandwich | Heterodimer | Nuclear receptor | Spine | Structural genomics | Structural proteomics in europe
