1g2n

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(New page: 200px<br /><applet load="1g2n" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g2n, resolution 1.65&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1g2n.gif|left|200px]]<br /><applet load="1g2n" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1g2n, resolution 1.65&Aring;" />
caption="1g2n, resolution 1.65&Aring;" />
'''CRYSTAL STRUCTURE OF THE LIGAND BINDING DOMAIN OF THE ULTRASPIRACLE PROTEIN USP, THE ORTHOLOG OF RXRS IN INSECTS'''<br />
'''CRYSTAL STRUCTURE OF THE LIGAND BINDING DOMAIN OF THE ULTRASPIRACLE PROTEIN USP, THE ORTHOLOG OF RXRS IN INSECTS'''<br />
==Overview==
==Overview==
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The major postembryonic developmental events happening in insect life, including molting and metamorphosis, are regulated and coordinated, temporally by pulses of ecdysone. The biological activity of this steroid, hormone is mediated by two nuclear receptors: the ecdysone receptor (EcR), and the Ultraspiracle protein (USP). The crystal structure of the, ligand-binding domain from the lepidopteran Heliothis virescens USP, reported here shows that the loop connecting helices H1 and H3 precludes, the canonical agonist conformation. The key residues that stabilize this, unique loop conformation are strictly conserved within the lepidopteran, USP family. The presence of an unexpected bound ligand that drives an, unusual antagonist conformation confirms the induced-fit mechanism, accompanying the ligand binding. The ligand-binding pocket exhibits a, retinoid X receptor-like anchoring part near a conserved arginine, which, could interact with a USP ligand functional group. The structure of this, receptor provides the template for designing inhibitors, which could be, utilized as a novel type of environmentally safe insecticides.
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The major postembryonic developmental events happening in insect life, including molting and metamorphosis, are regulated and coordinated temporally by pulses of ecdysone. The biological activity of this steroid hormone is mediated by two nuclear receptors: the ecdysone receptor (EcR) and the Ultraspiracle protein (USP). The crystal structure of the ligand-binding domain from the lepidopteran Heliothis virescens USP reported here shows that the loop connecting helices H1 and H3 precludes the canonical agonist conformation. The key residues that stabilize this unique loop conformation are strictly conserved within the lepidopteran USP family. The presence of an unexpected bound ligand that drives an unusual antagonist conformation confirms the induced-fit mechanism accompanying the ligand binding. The ligand-binding pocket exhibits a retinoid X receptor-like anchoring part near a conserved arginine, which could interact with a USP ligand functional group. The structure of this receptor provides the template for designing inhibitors, which could be utilized as a novel type of environmentally safe insecticides.
==About this Structure==
==About this Structure==
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1G2N is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Heliothis_virescens Heliothis virescens] with EPH as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1G2N OCA].
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1G2N is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Heliothis_virescens Heliothis virescens] with <scene name='pdbligand=EPH:'>EPH</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G2N OCA].
==Reference==
==Reference==
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[[Category: Heliothis virescens]]
[[Category: Heliothis virescens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Billas, I.M.L.]]
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[[Category: Billas, I M.L.]]
[[Category: Moras, D.]]
[[Category: Moras, D.]]
[[Category: Moulinier, L.]]
[[Category: Moulinier, L.]]
[[Category: Rochel, N.]]
[[Category: Rochel, N.]]
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[[Category: SPINE, Structural.Proteomics.in.Europe.]]
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[[Category: SPINE, Structural Proteomics in Europe.]]
[[Category: EPH]]
[[Category: EPH]]
[[Category: antiparallel alpha-helical sandwich]]
[[Category: antiparallel alpha-helical sandwich]]
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[[Category: structural proteomics in europe]]
[[Category: structural proteomics in europe]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 00:44:20 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:45:26 2008''

Revision as of 10:45, 21 February 2008


1g2n, resolution 1.65Å

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CRYSTAL STRUCTURE OF THE LIGAND BINDING DOMAIN OF THE ULTRASPIRACLE PROTEIN USP, THE ORTHOLOG OF RXRS IN INSECTS

Overview

The major postembryonic developmental events happening in insect life, including molting and metamorphosis, are regulated and coordinated temporally by pulses of ecdysone. The biological activity of this steroid hormone is mediated by two nuclear receptors: the ecdysone receptor (EcR) and the Ultraspiracle protein (USP). The crystal structure of the ligand-binding domain from the lepidopteran Heliothis virescens USP reported here shows that the loop connecting helices H1 and H3 precludes the canonical agonist conformation. The key residues that stabilize this unique loop conformation are strictly conserved within the lepidopteran USP family. The presence of an unexpected bound ligand that drives an unusual antagonist conformation confirms the induced-fit mechanism accompanying the ligand binding. The ligand-binding pocket exhibits a retinoid X receptor-like anchoring part near a conserved arginine, which could interact with a USP ligand functional group. The structure of this receptor provides the template for designing inhibitors, which could be utilized as a novel type of environmentally safe insecticides.

About this Structure

1G2N is a Single protein structure of sequence from Heliothis virescens with as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of the ligand-binding domain of the ultraspiracle protein USP, the ortholog of retinoid X receptors in insects., Billas IM, Moulinier L, Rochel N, Moras D, J Biol Chem. 2001 Mar 9;276(10):7465-74. Epub 2000 Oct 26. PMID:11053444

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