Solution Structures of PPARγ2/RXRα Complexes
PPARγ is a key regulator of glucose homeostasis and insulin sensitization. PPARγ must heterodimerize with its dimeric partner, the retinoid X receptor (RXR), to bind DNA and associated coactivators such as p160 family members or PGC-1α to regulate gene networks. To understand how coactivators are re...
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| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
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Wiley
2012-01-01
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| Series: | PPAR Research |
| Online Access: | http://dx.doi.org/10.1155/2012/701412 |
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| _version_ | 1832561906011865088 |
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| author | Judit Osz Maxim V. Pethoukhov Serena Sirigu Dmitri I. Svergun Dino Moras Natacha Rochel |
| author_facet | Judit Osz Maxim V. Pethoukhov Serena Sirigu Dmitri I. Svergun Dino Moras Natacha Rochel |
| author_sort | Judit Osz |
| collection | DOAJ |
| description | PPARγ is a key regulator of glucose homeostasis and insulin sensitization. PPARγ must heterodimerize with its dimeric partner, the retinoid X receptor (RXR), to bind DNA and associated coactivators such as p160 family members or PGC-1α to regulate gene networks. To understand how coactivators are recognized by the functional heterodimer PPARγ/RXRα and to determine the topological organization of the complexes, we performed a structural study using small angle X-ray scattering of PPARγ/RXRα in complex with DNA from regulated gene and the TIF2 receptor interacting domain (RID). The solution structures reveal an asymmetry of the overall structure due to the crucial role of the DNA in positioning the heterodimer and indicate asymmetrical binding of TIF2 to the heterodimer. |
| format | Article |
| id | doaj-art-37fafe4c9c85467caf1a2db477b8300a |
| institution | Kabale University |
| issn | 1687-4757 1687-4765 |
| language | English |
| publishDate | 2012-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | PPAR Research |
| spelling | doaj-art-37fafe4c9c85467caf1a2db477b8300a2025-02-03T01:23:49ZengWileyPPAR Research1687-47571687-47652012-01-01201210.1155/2012/701412701412Solution Structures of PPARγ2/RXRα ComplexesJudit Osz0Maxim V. Pethoukhov1Serena Sirigu2Dmitri I. Svergun3Dino Moras4Natacha Rochel5Department of Integrative Structural Biology, Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Centre National de Recherche Scientifique (CNRS) UMR 7104, Institut National de Santé et de Recherche Médicale (INSERM) U964, Université de Strasbourg, 67404 Illkirch, FranceThe European Molecular Biology Laboratory, Hamburg Outstation, 22603 Hamburg, GermanyDepartment of Integrative Structural Biology, Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Centre National de Recherche Scientifique (CNRS) UMR 7104, Institut National de Santé et de Recherche Médicale (INSERM) U964, Université de Strasbourg, 67404 Illkirch, FranceThe European Molecular Biology Laboratory, Hamburg Outstation, 22603 Hamburg, GermanyDepartment of Integrative Structural Biology, Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Centre National de Recherche Scientifique (CNRS) UMR 7104, Institut National de Santé et de Recherche Médicale (INSERM) U964, Université de Strasbourg, 67404 Illkirch, FranceDepartment of Integrative Structural Biology, Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Centre National de Recherche Scientifique (CNRS) UMR 7104, Institut National de Santé et de Recherche Médicale (INSERM) U964, Université de Strasbourg, 67404 Illkirch, FrancePPARγ is a key regulator of glucose homeostasis and insulin sensitization. PPARγ must heterodimerize with its dimeric partner, the retinoid X receptor (RXR), to bind DNA and associated coactivators such as p160 family members or PGC-1α to regulate gene networks. To understand how coactivators are recognized by the functional heterodimer PPARγ/RXRα and to determine the topological organization of the complexes, we performed a structural study using small angle X-ray scattering of PPARγ/RXRα in complex with DNA from regulated gene and the TIF2 receptor interacting domain (RID). The solution structures reveal an asymmetry of the overall structure due to the crucial role of the DNA in positioning the heterodimer and indicate asymmetrical binding of TIF2 to the heterodimer.http://dx.doi.org/10.1155/2012/701412 |
| spellingShingle | Judit Osz Maxim V. Pethoukhov Serena Sirigu Dmitri I. Svergun Dino Moras Natacha Rochel Solution Structures of PPARγ2/RXRα Complexes PPAR Research |
| title | Solution Structures of PPARγ2/RXRα Complexes |
| title_full | Solution Structures of PPARγ2/RXRα Complexes |
| title_fullStr | Solution Structures of PPARγ2/RXRα Complexes |
| title_full_unstemmed | Solution Structures of PPARγ2/RXRα Complexes |
| title_short | Solution Structures of PPARγ2/RXRα Complexes |
| title_sort | solution structures of pparγ2 rxrα complexes |
| url | http://dx.doi.org/10.1155/2012/701412 |
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