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1r1k

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[[Image:1r1k.gif|left|200px]]<br /><applet load="1r1k" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1r1k.gif|left|200px]]
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caption="1r1k, resolution 2.90&Aring;" />
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'''Crystal structure of the ligand-binding domains of the heterodimer EcR/USP bound to ponasterone A'''<br />
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{{Structure
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|PDB= 1r1k |SIZE=350|CAPTION= <scene name='initialview01'>1r1k</scene>, resolution 2.90&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=P1A:2,3,14,20,22-PENTAHYDROXYCHOLEST-7-EN-6-ONE'>P1A</scene> and <scene name='pdbligand=EPH:L-ALPHA-PHOSPHATIDYL-BETA-OLEOYL-GAMMA-PALMITOYL-PHOSPHATIDYLETHANOLAMINE'>EPH</scene>
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|ACTIVITY=
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|GENE= ECR OR NR1H1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7102 Heliothis virescens])
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}}
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'''Crystal structure of the ligand-binding domains of the heterodimer EcR/USP bound to ponasterone A'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1R1K 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=P1A:'>P1A</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=1R1K OCA].
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1R1K is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Heliothis_virescens Heliothis virescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R1K OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14595375 14595375]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/14595375 14595375]
[[Category: Heliothis virescens]]
[[Category: Heliothis virescens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: nuclear receptor]]
[[Category: nuclear receptor]]
[[Category: spine]]
[[Category: spine]]
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[[Category: structural genomics]]
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[[Category: structural genomic]]
[[Category: structural proteomics in europe]]
[[Category: structural proteomics in europe]]
[[Category: transcription regulation]]
[[Category: transcription regulation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:46:00 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:45:35 2008''

Revision as of 11:45, 20 March 2008

Image:1r1k.gif


PDB ID 1r1k

Drag the structure with the mouse to rotate
, resolution 2.90Å
Ligands: and
Gene: ECR OR NR1H1 (Heliothis virescens)
Coordinates: save as pdb, mmCIF, xml



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


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

1R1K 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

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