The conformational stability of pro-apoptotic BAX is dictated by discrete residues of the protein core
The pro-apoptotic BAX protein is a monomer under homeostatic conditions and, in response to stress, transforms into oligomers that induce apoptosis. Here, the authors characterize structural features of BAX that individually stabilize the monomer while collectively contributing to oligomerization.
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2021-08-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-021-25200-7 |
| _version_ | 1818430559901188096 |
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| author | Noah B. Bloch Thomas E. Wales Michelle S. Prew Hannah R. Levy John R. Engen Loren D. Walensky |
| author_facet | Noah B. Bloch Thomas E. Wales Michelle S. Prew Hannah R. Levy John R. Engen Loren D. Walensky |
| author_sort | Noah B. Bloch |
| collection | DOAJ |
| description | The pro-apoptotic BAX protein is a monomer under homeostatic conditions and, in response to stress, transforms into oligomers that induce apoptosis. Here, the authors characterize structural features of BAX that individually stabilize the monomer while collectively contributing to oligomerization. |
| first_indexed | 2024-12-14T15:35:21Z |
| format | Article |
| id | doaj.art-6094840e65e043afbdbb1d1b24daacd6 |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-12-14T15:35:21Z |
| publishDate | 2021-08-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-6094840e65e043afbdbb1d1b24daacd62022-12-21T22:55:44ZengNature PortfolioNature Communications2041-17232021-08-0112111210.1038/s41467-021-25200-7The conformational stability of pro-apoptotic BAX is dictated by discrete residues of the protein coreNoah B. Bloch0Thomas E. Wales1Michelle S. Prew2Hannah R. Levy3John R. Engen4Loren D. Walensky5Department of Pediatric Oncology, Dana-Farber Cancer InstituteDepartment of Chemistry and Chemical Biology, Northeastern UniversityDepartment of Pediatric Oncology, Dana-Farber Cancer InstituteDepartment of Pediatric Oncology, Dana-Farber Cancer InstituteDepartment of Chemistry and Chemical Biology, Northeastern UniversityDepartment of Pediatric Oncology, Dana-Farber Cancer InstituteThe pro-apoptotic BAX protein is a monomer under homeostatic conditions and, in response to stress, transforms into oligomers that induce apoptosis. Here, the authors characterize structural features of BAX that individually stabilize the monomer while collectively contributing to oligomerization.https://doi.org/10.1038/s41467-021-25200-7 |
| spellingShingle | Noah B. Bloch Thomas E. Wales Michelle S. Prew Hannah R. Levy John R. Engen Loren D. Walensky The conformational stability of pro-apoptotic BAX is dictated by discrete residues of the protein core Nature Communications |
| title | The conformational stability of pro-apoptotic BAX is dictated by discrete residues of the protein core |
| title_full | The conformational stability of pro-apoptotic BAX is dictated by discrete residues of the protein core |
| title_fullStr | The conformational stability of pro-apoptotic BAX is dictated by discrete residues of the protein core |
| title_full_unstemmed | The conformational stability of pro-apoptotic BAX is dictated by discrete residues of the protein core |
| title_short | The conformational stability of pro-apoptotic BAX is dictated by discrete residues of the protein core |
| title_sort | conformational stability of pro apoptotic bax is dictated by discrete residues of the protein core |
| url | https://doi.org/10.1038/s41467-021-25200-7 |
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