Structural basis for recognition of 53BP1 tandem Tudor domain by TIRR
The p53-binding protein 1 (53BP1) regulates the choice of the DNA double-strand break repair pathway. Here the authors present the crystal structure of Tudor-interacting repair regulator (TIRR) bound to the 53BP1 tandem Tudor domain, which reveals how TIRR blocks H4K20me2 binding to 53BP1 Tudor and...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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Nature Portfolio
2018-05-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-018-04557-2 |
| _version_ | 1819039815075627008 |
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| author | Yaxin Dai Aili Zhang Shan Shan Zihua Gong Zheng Zhou |
| author_facet | Yaxin Dai Aili Zhang Shan Shan Zihua Gong Zheng Zhou |
| author_sort | Yaxin Dai |
| collection | DOAJ |
| description | The p53-binding protein 1 (53BP1) regulates the choice of the DNA double-strand break repair pathway. Here the authors present the crystal structure of Tudor-interacting repair regulator (TIRR) bound to the 53BP1 tandem Tudor domain, which reveals how TIRR blocks H4K20me2 binding to 53BP1 Tudor and functionally differs from its paralog Nudt16. |
| first_indexed | 2024-12-21T08:59:12Z |
| format | Article |
| id | doaj.art-10e5474c6f744b3e827891e12f49cc88 |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-12-21T08:59:12Z |
| publishDate | 2018-05-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-10e5474c6f744b3e827891e12f49cc882022-12-21T19:09:29ZengNature PortfolioNature Communications2041-17232018-05-019111210.1038/s41467-018-04557-2Structural basis for recognition of 53BP1 tandem Tudor domain by TIRRYaxin Dai0Aili Zhang1Shan Shan2Zihua Gong3Zheng Zhou4National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of SciencesDepartment of Cancer Biology, Cleveland Clinic Lerner Research InstituteNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of SciencesDepartment of Cancer Biology, Cleveland Clinic Lerner Research InstituteNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of SciencesThe p53-binding protein 1 (53BP1) regulates the choice of the DNA double-strand break repair pathway. Here the authors present the crystal structure of Tudor-interacting repair regulator (TIRR) bound to the 53BP1 tandem Tudor domain, which reveals how TIRR blocks H4K20me2 binding to 53BP1 Tudor and functionally differs from its paralog Nudt16.https://doi.org/10.1038/s41467-018-04557-2 |
| spellingShingle | Yaxin Dai Aili Zhang Shan Shan Zihua Gong Zheng Zhou Structural basis for recognition of 53BP1 tandem Tudor domain by TIRR Nature Communications |
| title | Structural basis for recognition of 53BP1 tandem Tudor domain by TIRR |
| title_full | Structural basis for recognition of 53BP1 tandem Tudor domain by TIRR |
| title_fullStr | Structural basis for recognition of 53BP1 tandem Tudor domain by TIRR |
| title_full_unstemmed | Structural basis for recognition of 53BP1 tandem Tudor domain by TIRR |
| title_short | Structural basis for recognition of 53BP1 tandem Tudor domain by TIRR |
| title_sort | structural basis for recognition of 53bp1 tandem tudor domain by tirr |
| url | https://doi.org/10.1038/s41467-018-04557-2 |
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