1g5y
From Proteopedia
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| - | [[Image:1g5y.jpg|left|200px]] | + | [[Image:1g5y.jpg|left|200px]] |
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| - | '''THE 2.0 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF THE RXRALPHA LIGAND BINDING DOMAIN TETRAMER IN THE PRESENCE OF A NON-ACTIVATING RETINOIC ACID ISOMER.''' | + | {{Structure |
| + | |PDB= 1g5y |SIZE=350|CAPTION= <scene name='initialview01'>1g5y</scene>, resolution 2.00Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=REA:RETINOIC ACID'>REA</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''THE 2.0 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF THE RXRALPHA LIGAND BINDING DOMAIN TETRAMER IN THE PRESENCE OF A NON-ACTIVATING RETINOIC ACID ISOMER.''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1G5Y is a [ | + | 1G5Y is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G5Y OCA]. |
==Reference== | ==Reference== | ||
| - | Structural basis for autorepression of retinoid X receptor by tetramer formation and the AF-2 helix., Gampe RT Jr, Montana VG, Lambert MH, Wisely GB, Milburn MV, Xu HE, Genes Dev. 2000 Sep 1;14(17):2229-41. PMID:[http:// | + | Structural basis for autorepression of retinoid X receptor by tetramer formation and the AF-2 helix., Gampe RT Jr, Montana VG, Lambert MH, Wisely GB, Milburn MV, Xu HE, Genes Dev. 2000 Sep 1;14(17):2229-41. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10970886 10970886] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: rxralpha ligand binding domain]] | [[Category: rxralpha ligand binding domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:18:38 2008'' |
Revision as of 09:18, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE 2.0 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF THE RXRALPHA LIGAND BINDING DOMAIN TETRAMER IN THE PRESENCE OF A NON-ACTIVATING RETINOIC ACID ISOMER.
Overview
The 9-cis-retinoic acid receptors (RXRalpha, RXRbeta, and RXRgamma) are nuclear receptors that play key roles in multiple hormone-signaling pathways. Biochemical data indicate that, in the absence of ligand, RXR can exist as an inactive tetramer and that its dissociation, induced by ligand, is important for receptor activation. In this article we report the inactivated tetramer structures of the RXRalpha ligand-binding domain (LBD), either in the absence of or in the presence of a nonactivating ligand. These structures reveal that the RXR LBD tetramer forms a compact, disc-shaped complex, consisting of two symmetric dimers that are packed along helices 3 and 11. In each monomer, the AF-2 helix protrudes away from the core domain and spans into the coactivator binding site in the adjacent monomer of the symmetric dimer. In this configuration, the AF-2 helix physically excludes the binding of coactivators and suggests an autorepression mechanism that is mediated by the AF-2 helix within the tetramer. The RXR-tetramer interface is assembled from amino acids that are conserved across several closely related receptors, including the HNF4s and COUP transcription factors, and may therefore provide a model for understanding structure and regulation of this subfamily of nuclear receptors.
About this Structure
1G5Y is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural basis for autorepression of retinoid X receptor by tetramer formation and the AF-2 helix., Gampe RT Jr, Montana VG, Lambert MH, Wisely GB, Milburn MV, Xu HE, Genes Dev. 2000 Sep 1;14(17):2229-41. PMID:10970886
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