Topology and structure of an engineered human cohesin complex bound to Pds5B
Cohesin is a ring-shaped protein complex that structures chromatin and mediates sister chromatid cohesion. Here the authors rigidify cohesin using engineered Smc1 and Smc3 and generated 3D models showing how Pds5B forms an integral part of the cohesin ring.
| Main Authors: | , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2016-08-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/ncomms12523 |
| _version_ | 1818952103538720768 |
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| author | Michael T. Hons Pim J. Huis in ‘t Veld Jan Kaesler Pascaline Rombaut Alexander Schleiffer Franz Herzog Holger Stark Jan-Michael Peters |
| author_facet | Michael T. Hons Pim J. Huis in ‘t Veld Jan Kaesler Pascaline Rombaut Alexander Schleiffer Franz Herzog Holger Stark Jan-Michael Peters |
| author_sort | Michael T. Hons |
| collection | DOAJ |
| description | Cohesin is a ring-shaped protein complex that structures chromatin and mediates sister chromatid cohesion. Here the authors rigidify cohesin using engineered Smc1 and Smc3 and generated 3D models showing how Pds5B forms an integral part of the cohesin ring. |
| first_indexed | 2024-12-20T09:45:03Z |
| format | Article |
| id | doaj.art-0f7233fdcb064b2d901ef3b4d2d7f3bf |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-12-20T09:45:03Z |
| publishDate | 2016-08-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-0f7233fdcb064b2d901ef3b4d2d7f3bf2022-12-21T19:44:45ZengNature PortfolioNature Communications2041-17232016-08-017111110.1038/ncomms12523Topology and structure of an engineered human cohesin complex bound to Pds5BMichael T. Hons0Pim J. Huis in ‘t Veld1Jan Kaesler2Pascaline Rombaut3Alexander Schleiffer4Franz Herzog5Holger Stark6Jan-Michael Peters7Department of Structural Dynamics, Max Planck Institute for Biophysical ChemistryResearch Institute of Molecular Pathology (IMP)Department of Structural Dynamics, Max Planck Institute for Biophysical ChemistryDepartment of Biochemistry, Gene Center, Ludwig-Maximilian UniversityResearch Institute of Molecular Pathology (IMP)Department of Biochemistry, Gene Center, Ludwig-Maximilian UniversityDepartment of Structural Dynamics, Max Planck Institute for Biophysical ChemistryResearch Institute of Molecular Pathology (IMP)Cohesin is a ring-shaped protein complex that structures chromatin and mediates sister chromatid cohesion. Here the authors rigidify cohesin using engineered Smc1 and Smc3 and generated 3D models showing how Pds5B forms an integral part of the cohesin ring.https://doi.org/10.1038/ncomms12523 |
| spellingShingle | Michael T. Hons Pim J. Huis in ‘t Veld Jan Kaesler Pascaline Rombaut Alexander Schleiffer Franz Herzog Holger Stark Jan-Michael Peters Topology and structure of an engineered human cohesin complex bound to Pds5B Nature Communications |
| title | Topology and structure of an engineered human cohesin complex bound to Pds5B |
| title_full | Topology and structure of an engineered human cohesin complex bound to Pds5B |
| title_fullStr | Topology and structure of an engineered human cohesin complex bound to Pds5B |
| title_full_unstemmed | Topology and structure of an engineered human cohesin complex bound to Pds5B |
| title_short | Topology and structure of an engineered human cohesin complex bound to Pds5B |
| title_sort | topology and structure of an engineered human cohesin complex bound to pds5b |
| url | https://doi.org/10.1038/ncomms12523 |
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