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1r20

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Revision as of 08:08, 28 February 2018

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

Structural highlights

1r20 is a 2 chain structure with sequence from Chloridea virescens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	1r1k
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ECR_HELVI] Receptor for ecdysone. Binds to ecdysone response elements (ECRES) (By similarity).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Billas IM, Iwema T, Garnier JM, Mitschler A, Rochel N, Moras D. Structural adaptability in the ligand-binding pocket of the ecdysone hormone receptor. Nature. 2003 Nov 6;426(6962):91-6. Epub 2003 Nov 2. PMID:14595375 doi:10.1038/nature02112

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1r20"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the ligand-binding domains of the heterodimer EcR/USP bound to the synthetic agonist BYI06830==
 <StructureSection load='1r20' size='340' side='right' caption='[[1r20]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1r20]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Helvi Helvi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R20 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1R20 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1r20]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Chloridea_virescens Chloridea virescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R20 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1R20 FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EPH:L-ALPHA-PHOSPHATIDYL-BETA-OLEOYL-GAMMA-PALMITOYL-PHOSPHATIDYLETHANOLAMINE'>EPH</scene>, <scene name='pdbligand=HWG:N-(TERT-BUTYL)-3,5-DIMETHYL-N-[(5-METHYL-2,3-DIHYDRO-1,4-BENZODIOXIN-6-YL)CARBONYL]BENZOHYDRAZIDE'>HWG</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1r1k|1r1k]]</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1r20 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r20 OCA], [http://pdbe.org/1r20 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1r20 RCSB], [http://www.ebi.ac.uk/pdbsum/1r20 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1r20 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r20 OCA], [http://pdbe.org/1r20 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1r20 RCSB], [http://www.ebi.ac.uk/pdbsum/1r20 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1r20 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 13: / Line 14: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/r2/1r20_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/r2/1r20_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 32: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Helvi]]
+[[Category: Chloridea virescens]]
 [[Category: Billas, I M.L]]
 [[Category: Garnier, J M]]

1r20

From Proteopedia

Revision as of 08:08, 28 February 2018

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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