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1hg4

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Revision as of 09:10, 10 January 2018

Ultraspiracle ligand binding domain from Drosophila melanogaster

Structural highlights

1hg4 is a 6 chain structure with sequence from Drome. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[USP_DROME] Receptor for ecdysone. May be an important modulator of insect metamorphosis. Plays an important part in embryonic and post-embryonic development. Binds to ecdysone response elements (ECRES) such as in the promoter region of s15 chorion gene.

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

Ultraspiracle (USP) is the invertebrate homologue of the mammalian retinoid X receptor (RXR). RXR plays a uniquely important role in differentiation, development, and homeostasis through its ability to serve as a heterodimeric partner to many other nuclear receptors. RXR is able to influence the activity of its partner receptors through the action of the ligand 9-cis retinoic acid. In contrast to RXR, USP has no known high-affinity ligand and is thought to be a silent component in the heterodimeric complex with partner receptors such as the ecdysone receptor. Here we report the 2.4-A crystal structure of the USP ligand-binding domain. The structure shows that a conserved sequence motif found in dipteran and lepidopteran USPs, but not in mammalian RXRs, serves to lock USP in an inactive conformation. It also shows that USP has a large hydrophobic cavity, implying that there is almost certainly a natural ligand for USP. This cavity is larger than that seen previously for most other nuclear receptors. Intriguingly, this cavity has partial occupancy by a bound lipid, which is likely to resemble the natural ligand for USP.

The structure of the ultraspiracle ligand-binding domain reveals a nuclear receptor locked in an inactive conformation.,Clayton GM, Peak-Chew SY, Evans RM, Schwabe JW Proc Natl Acad Sci U S A. 2001 Feb 13;98(4):1549-54. Epub 2001 Feb 6. PMID:11171988^[1]

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

References

↑ Clayton GM, Peak-Chew SY, Evans RM, Schwabe JW. The structure of the ultraspiracle ligand-binding domain reveals a nuclear receptor locked in an inactive conformation. Proc Natl Acad Sci U S A. 2001 Feb 13;98(4):1549-54. Epub 2001 Feb 6. PMID:11171988 doi:10.1073/pnas.041611298

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/1hg4"

@@ Line 1: / Line 1: @@
 ==Ultraspiracle ligand binding domain from Drosophila melanogaster==
 <StructureSection load='1hg4' size='340' side='right' caption='[[1hg4]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[1hg4]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HG4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HG4 FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LPP:2-(HEXADECANOYLOXY)-1-[(PHOSPHONOOXY)METHYL]ETHYL+HEXADECANOATE'>LPP</scene></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=1hg4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hg4 OCA], [http://pdbe.org/1hg4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hg4 RCSB], [http://www.ebi.ac.uk/pdbsum/1hg4 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=1hg4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hg4 OCA], [http://pdbe.org/1hg4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hg4 RCSB], [http://www.ebi.ac.uk/pdbsum/1hg4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1hg4 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 12: / Line 13: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hg/1hg4_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hg/1hg4_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

1hg4

From Proteopedia

Revision as of 09:10, 10 January 2018

Ultraspiracle ligand binding domain from Drosophila melanogaster

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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