1r20: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,438 edits
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 ...
 
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,438 edits
No edit summary
 
(16 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1r20.gif|left|200px]]<br /><applet load="1r20" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1r20, resolution 3.0&Aring;" />
'''Crystal structure of the ligand-binding domains of the heterodimer EcR/USP bound to the synthetic agonist BYI06830'''<br />


==Overview==
==Crystal structure of the ligand-binding domains of the heterodimer EcR/USP bound to the synthetic agonist BYI06830==
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.
<StructureSection load='1r20' size='340' side='right'caption='[[1r20]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1r20]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Heliothis_virescens Heliothis 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 [https://proteopedia.org/fgij/fg.htm?mol=1R20 FirstGlance]. <br>
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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1R20 OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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>
==Reference==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1r20 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r20 OCA], [https://pdbe.org/1r20 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r20 RCSB], [https://www.ebi.ac.uk/pdbsum/1r20 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r20 ProSAT]</span></td></tr>
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]
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q7SIF6_HELVI Q7SIF6_HELVI]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <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>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1r20 ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Heliothis virescens]]
[[Category: Heliothis virescens]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Billas, I.M.L.]]
[[Category: Billas IML]]
[[Category: Garnier, J.M.]]
[[Category: Garnier JM]]
[[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.Proteomics.in.Europe.]]
[[Category: EPH]]
[[Category: HWG]]
[[Category: alpha-helical sandwich]]
[[Category: heterodimer]]
[[Category: nuclear receptor]]
[[Category: spine]]
[[Category: structural genomics]]
[[Category: structural proteomics in europe]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:12:52 2007''
Retrieved from "https://proteopedia.org/1r20"