2han: Difference between revisions
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==Overview== | ==Overview== | ||
The heterodimer of the ecdysone receptor (EcR) and ultraspiracle (Usp), members of the nuclear receptors superfamily, is considered as the | 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. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: zinc finger]] | [[Category: zinc finger]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:39:54 2008'' | ||
Revision as of 18:39, 21 February 2008
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Structural basis of heterodimeric ecdysteroid receptor interaction with natural response element hsp27 gene promoter
OverviewOverview
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.
About this StructureAbout this Structure
2HAN is a Protein complex structure of sequences from Drosophila melanogaster with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
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
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