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2han

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Revision as of 08:09, 18 October 2017

Structural basis of heterodimeric ecdysteroid receptor interaction with natural response element hsp27 gene promoter

Structural highlights

2han is a 4 chain structure with sequence from Drome. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:	usp, Cf1, NR2B4 (DROME), EcR, NR1H1 (DROME)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ECR_DROME] Receptor for ecdysone. Binds to ecdysone response elements (ECRES) following ecdysone-binding, and recruitment of a complex containing the histone methyltransferase trr, leads to activate transcription of target genes.^[1] [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

The heterodimer of the ecdysone receptor (EcR) and ultraspiracle (Usp), members of the nuclear receptors superfamily, is considered as the functional receptor for ecdysteroids initiating molting and metamorphosis in insects. Here we report the 1.95 A structure of the complex formed by the DNA-binding domains (DBDs) the EcR and the Usp, bound to the natural pseudopalindromic response element. Comparison of the structure with that obtained previously, using an idealized response element, shows how the EcRDBD, which has been previously reported to possess extraordinary flexibility, accommodates DNA-induced structural changes. Part of the C-terminal extension (CTE) of the EcRDBD folds into an alpha-helix whose location in the minor groove does not match any of the locations previously observed for nuclear receptors. Mutational analyses suggest that the alpha-helix is a component of EcR-box, a novel element indispensable for DNA-binding and located within the nuclear receptor CTE. This element seems to be a general feature of all known EcRs.

Novel DNA-binding element within the C-terminal extension of the nuclear receptor DNA-binding domain.,Jakob M, Kolodziejczyk R, Orlowski M, Krzywda S, Kowalska A, Dutko-Gwozdz J, Gwozdz T, Kochman M, Jaskolski M, Ozyhar A Nucleic Acids Res. 2007;35(8):2705-18. Epub 2007 Apr 10. PMID:17426125^[2]

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

References

↑ Koelle MR, Talbot WS, Segraves WA, Bender MT, Cherbas P, Hogness DS. The Drosophila EcR gene encodes an ecdysone receptor, a new member of the steroid receptor superfamily. Cell. 1991 Oct 4;67(1):59-77. PMID:1913820
↑ Jakob M, Kolodziejczyk R, Orlowski M, Krzywda S, Kowalska A, Dutko-Gwozdz J, Gwozdz T, Kochman M, Jaskolski M, Ozyhar A. Novel DNA-binding element within the C-terminal extension of the nuclear receptor DNA-binding domain. Nucleic Acids Res. 2007;35(8):2705-18. Epub 2007 Apr 10. PMID:17426125 doi:10.1093/nar/gkm162

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/2han"

@@ Line 1: / Line 1: @@
 ==Structural basis of heterodimeric ecdysteroid receptor interaction with natural response element hsp27 gene promoter==
 <StructureSection load='2han' size='340' side='right' caption='[[2han]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">usp, Cf1, NR2B4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME]), EcR, NR1H1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</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=2han FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2han OCA], [http://pdbe.org/2han PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2han RCSB], [http://www.ebi.ac.uk/pdbsum/2han 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=2han FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2han OCA], [http://pdbe.org/2han PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2han RCSB], [http://www.ebi.ac.uk/pdbsum/2han PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2han ProSAT]</span></td></tr>
 </table>
 == Function ==

2han

From Proteopedia

Revision as of 08:09, 18 October 2017

Structural basis of heterodimeric ecdysteroid receptor interaction with natural response element hsp27 gene promoter

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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