The quaternary architecture of RARβ–RXRα heterodimer facilitates domain–domain signal transmission
Nuclear receptors (NR) are multidomain proteins, which makes their crystallization challenging. Here the authors present the crystal structure of the retinoic acid receptor β–retinoic X receptor α (RARβ–RXRα) heterodimer bound to DNA, ligands and coactivator peptides, which shows that NR quaternary...
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
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Nature Portfolio
2017-10-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-017-00981-y |
| _version_ | 1818427400354004992 |
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| author | Vikas Chandra Dalei Wu Sheng Li Nalini Potluri Youngchang Kim Fraydoon Rastinejad |
| author_facet | Vikas Chandra Dalei Wu Sheng Li Nalini Potluri Youngchang Kim Fraydoon Rastinejad |
| author_sort | Vikas Chandra |
| collection | DOAJ |
| description | Nuclear receptors (NR) are multidomain proteins, which makes their crystallization challenging. Here the authors present the crystal structure of the retinoic acid receptor β–retinoic X receptor α (RARβ–RXRα) heterodimer bound to DNA, ligands and coactivator peptides, which shows that NR quaternary architectures are variable. |
| first_indexed | 2024-12-14T14:45:07Z |
| format | Article |
| id | doaj.art-a6df162dc85447f4af921752869d12fa |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-12-14T14:45:07Z |
| publishDate | 2017-10-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-a6df162dc85447f4af921752869d12fa2022-12-21T22:57:19ZengNature PortfolioNature Communications2041-17232017-10-01811910.1038/s41467-017-00981-yThe quaternary architecture of RARβ–RXRα heterodimer facilitates domain–domain signal transmissionVikas Chandra0Dalei Wu1Sheng Li2Nalini Potluri3Youngchang Kim4Fraydoon Rastinejad5Integrative Metabolism Program, Sanford Burnham Prebys Medical Discovery InstituteIntegrative Metabolism Program, Sanford Burnham Prebys Medical Discovery InstituteDepartment of Medicine and UCSD DXMS Proteomics Resource, University of California, San DiegoIntegrative Metabolism Program, Sanford Burnham Prebys Medical Discovery InstituteStructural Biology Center, Biosciences Division, Argonne National LaboratoryIntegrative Metabolism Program, Sanford Burnham Prebys Medical Discovery InstituteNuclear receptors (NR) are multidomain proteins, which makes their crystallization challenging. Here the authors present the crystal structure of the retinoic acid receptor β–retinoic X receptor α (RARβ–RXRα) heterodimer bound to DNA, ligands and coactivator peptides, which shows that NR quaternary architectures are variable.https://doi.org/10.1038/s41467-017-00981-y |
| spellingShingle | Vikas Chandra Dalei Wu Sheng Li Nalini Potluri Youngchang Kim Fraydoon Rastinejad The quaternary architecture of RARβ–RXRα heterodimer facilitates domain–domain signal transmission Nature Communications |
| title | The quaternary architecture of RARβ–RXRα heterodimer facilitates domain–domain signal transmission |
| title_full | The quaternary architecture of RARβ–RXRα heterodimer facilitates domain–domain signal transmission |
| title_fullStr | The quaternary architecture of RARβ–RXRα heterodimer facilitates domain–domain signal transmission |
| title_full_unstemmed | The quaternary architecture of RARβ–RXRα heterodimer facilitates domain–domain signal transmission |
| title_short | The quaternary architecture of RARβ–RXRα heterodimer facilitates domain–domain signal transmission |
| title_sort | quaternary architecture of rarβ rxrα heterodimer facilitates domain domain signal transmission |
| url | https://doi.org/10.1038/s41467-017-00981-y |
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