<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</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/chain_selection.php?pdb_ID=2ata ConSurf].
</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=2han ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
Revision as of 04:34, 8 February 2016
Structural basis of heterodimeric ecdysteroid receptor interaction with natural response element hsp27 gene promoter
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.
[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
