1r0n

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(New page: 200px<br /> <applet load="1r0n" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r0n, resolution 2.60&Aring;" /> '''Crystal Structure o...)
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<applet load="1r0n" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1r0n, resolution 2.60&Aring;" />
caption="1r0n, resolution 2.60&Aring;" />
'''Crystal Structure of Heterodimeric Ecdsyone receptor DNA binding complex'''<br />
'''Crystal Structure of Heterodimeric Ecdsyone receptor DNA binding complex'''<br />
==Overview==
==Overview==
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Ecdysteroids initiate molting and metamorphosis in insects via a, heterodimeric receptor consisting of the ecdysone receptor (EcR) and, ultraspiracle (USP). The EcR-USP heterodimer preferentially mediates, transcription through highly degenerate pseudo-palindromic response, elements, resembling inverted repeats of 5'-AGGTCA-3' separated by 1 bp, (IR-1). The requirement for a heterodimeric arrangement of EcR-USP, subunits to bind to a symmetric DNA is unusual within the nuclear receptor, superfamily. We describe the 2.24 A structure of the EcR-USP DNA-binding, domain (DBD) heterodimer bound to an idealized IR-1 element. EcR and USP, use similar surfaces, and rely on the deformed minor groove of the DNA to, establish protein-protein contacts. As retinoid X receptor (RXR) is the, mammalian homolog of USP, we also solved the 2.60 A crystal structure of, the EcR-RXR DBD heterodimer on IR-1 and found the dimerization and, DNA-binding interfaces to be the same as in the EcR-USP complex. Sequence, alignments indicate that the EcR-RXR heterodimer is an important model for, understanding how the FXR-RXR heterodimer binds to IR-1 sites.
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Ecdysteroids initiate molting and metamorphosis in insects via a heterodimeric receptor consisting of the ecdysone receptor (EcR) and ultraspiracle (USP). The EcR-USP heterodimer preferentially mediates transcription through highly degenerate pseudo-palindromic response elements, resembling inverted repeats of 5'-AGGTCA-3' separated by 1 bp (IR-1). The requirement for a heterodimeric arrangement of EcR-USP subunits to bind to a symmetric DNA is unusual within the nuclear receptor superfamily. We describe the 2.24 A structure of the EcR-USP DNA-binding domain (DBD) heterodimer bound to an idealized IR-1 element. EcR and USP use similar surfaces, and rely on the deformed minor groove of the DNA to establish protein-protein contacts. As retinoid X receptor (RXR) is the mammalian homolog of USP, we also solved the 2.60 A crystal structure of the EcR-RXR DBD heterodimer on IR-1 and found the dimerization and DNA-binding interfaces to be the same as in the EcR-USP complex. Sequence alignments indicate that the EcR-RXR heterodimer is an important model for understanding how the FXR-RXR heterodimer binds to IR-1 sites.
==About this Structure==
==About this Structure==
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1R0N is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1R0N OCA].
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1R0N is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R0N OCA].
==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Devarakonda, S.]]
[[Category: Devarakonda, S.]]
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[[Category: Harp, J.M.]]
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[[Category: Harp, J M.]]
[[Category: Kim, Y.]]
[[Category: Kim, Y.]]
[[Category: Ozyhar, A.]]
[[Category: Ozyhar, A.]]
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[[Category: ultraspiracle]]
[[Category: ultraspiracle]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:58:17 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:45:44 2008''

Revision as of 12:45, 21 February 2008


1r0n, resolution 2.60Å

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Crystal Structure of Heterodimeric Ecdsyone receptor DNA binding complex

Overview

Ecdysteroids initiate molting and metamorphosis in insects via a heterodimeric receptor consisting of the ecdysone receptor (EcR) and ultraspiracle (USP). The EcR-USP heterodimer preferentially mediates transcription through highly degenerate pseudo-palindromic response elements, resembling inverted repeats of 5'-AGGTCA-3' separated by 1 bp (IR-1). The requirement for a heterodimeric arrangement of EcR-USP subunits to bind to a symmetric DNA is unusual within the nuclear receptor superfamily. We describe the 2.24 A structure of the EcR-USP DNA-binding domain (DBD) heterodimer bound to an idealized IR-1 element. EcR and USP use similar surfaces, and rely on the deformed minor groove of the DNA to establish protein-protein contacts. As retinoid X receptor (RXR) is the mammalian homolog of USP, we also solved the 2.60 A crystal structure of the EcR-RXR DBD heterodimer on IR-1 and found the dimerization and DNA-binding interfaces to be the same as in the EcR-USP complex. Sequence alignments indicate that the EcR-RXR heterodimer is an important model for understanding how the FXR-RXR heterodimer binds to IR-1 sites.

About this Structure

1R0N is a Protein complex structure of sequences from Drosophila melanogaster and Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

Structure of the heterodimeric ecdysone receptor DNA-binding complex., Devarakonda S, Harp JM, Kim Y, Ozyhar A, Rastinejad F, EMBO J. 2003 Nov 3;22(21):5827-40. PMID:14592980

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