1r20: Difference between revisions
From Proteopedia
Jump to navigationJump to search
New page: left|200px<br /><applet load="1r20" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r20, resolution 3.0Å" /> '''Crystal structure of ... |
No edit summary |
||
| Line 1: | Line 1: | ||
[[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'' | ||
