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1by4

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(New page: 200px<br /> <applet load="1by4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1by4, resolution 2.1&Aring;" /> '''STRUCTURE AND MECHAN...)
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<applet load="1by4" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1by4, resolution 2.1&Aring;" />
caption="1by4, resolution 2.1&Aring;" />
'''STRUCTURE AND MECHANISM OF THE HOMODIMERIC ASSEMBLY OF THE RXR ON DNA'''<br />
'''STRUCTURE AND MECHANISM OF THE HOMODIMERIC ASSEMBLY OF THE RXR ON DNA'''<br />
==Overview==
==Overview==
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The 9-cis retinoic acid receptor, RXR, binds DNA effectively as a, homodimer or as a heterodimer with other nuclear receptors. The, DNA-binding sites for these RXR complexes are direct repeats of a, consensus sequence separated by one to five base-pairs of intervening, space. Here, we report the 2.1 A crystal structure of the RXR-DNA-binding, domain as a homodimer in complex with its idealized direct repeat DNA, target. The structure shows how a gene-regulatory site can induce, conformational changes in a transcription factor that promote, homo-cooperative assembly. Specifically, an alpha-helix in the T-box is, disrupted to allow efficient DNA-binding and subunit dimerization. RXR, displays a relaxed mode of sequence recognition, interacting with only, three base-pairs in each hexameric half-site. The structure illustrates, how site selection is achieved in this large eukaryotic transcription, factor family through discrete protein-protein interactions and the use of, tandem DNA binding sites with characteristic spacings.
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The 9-cis retinoic acid receptor, RXR, binds DNA effectively as a homodimer or as a heterodimer with other nuclear receptors. The DNA-binding sites for these RXR complexes are direct repeats of a consensus sequence separated by one to five base-pairs of intervening space. Here, we report the 2.1 A crystal structure of the RXR-DNA-binding domain as a homodimer in complex with its idealized direct repeat DNA target. The structure shows how a gene-regulatory site can induce conformational changes in a transcription factor that promote homo-cooperative assembly. Specifically, an alpha-helix in the T-box is disrupted to allow efficient DNA-binding and subunit dimerization. RXR displays a relaxed mode of sequence recognition, interacting with only three base-pairs in each hexameric half-site. The structure illustrates how site selection is achieved in this large eukaryotic transcription factor family through discrete protein-protein interactions and the use of tandem DNA binding sites with characteristic spacings.
==About this Structure==
==About this Structure==
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1BY4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [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=1BY4 OCA].
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1BY4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [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=1BY4 OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Ahvazi, B.]]
[[Category: Ahvazi, B.]]
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[[Category: Chasse, S.A.]]
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[[Category: Chasse, S A.]]
[[Category: Devarakonda, S.]]
[[Category: Devarakonda, S.]]
[[Category: Rastinejad, F.]]
[[Category: Rastinejad, F.]]
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[[Category: Sierk, M.L.]]
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[[Category: Sierk, M L.]]
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[[Category: Sigler, P.B.]]
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[[Category: Sigler, P B.]]
[[Category: Zhao, Q.]]
[[Category: Zhao, Q.]]
[[Category: ZN]]
[[Category: ZN]]
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[[Category: rxr]]
[[Category: rxr]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:15:23 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:00:24 2008''

Revision as of 10:00, 21 February 2008


1by4, resolution 2.1Å

Drag the structure with the mouse to rotate

STRUCTURE AND MECHANISM OF THE HOMODIMERIC ASSEMBLY OF THE RXR ON DNA

Overview

The 9-cis retinoic acid receptor, RXR, binds DNA effectively as a homodimer or as a heterodimer with other nuclear receptors. The DNA-binding sites for these RXR complexes are direct repeats of a consensus sequence separated by one to five base-pairs of intervening space. Here, we report the 2.1 A crystal structure of the RXR-DNA-binding domain as a homodimer in complex with its idealized direct repeat DNA target. The structure shows how a gene-regulatory site can induce conformational changes in a transcription factor that promote homo-cooperative assembly. Specifically, an alpha-helix in the T-box is disrupted to allow efficient DNA-binding and subunit dimerization. RXR displays a relaxed mode of sequence recognition, interacting with only three base-pairs in each hexameric half-site. The structure illustrates how site selection is achieved in this large eukaryotic transcription factor family through discrete protein-protein interactions and the use of tandem DNA binding sites with characteristic spacings.

About this Structure

1BY4 is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

Structural basis of RXR-DNA interactions., Zhao Q, Chasse SA, Devarakonda S, Sierk ML, Ahvazi B, Rastinejad F, J Mol Biol. 2000 Feb 18;296(2):509-20. PMID:10669605

Page seeded by OCA on Thu Feb 21 12:00:24 2008

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