The anti-apoptotic Bcl-x(L) protein, a new piece in the puzzle of cytochrome c interactome.
A structural model of the adduct between human cytochrome c and the human anti-apoptotic protein Bcl-x(L), which defines the protein-protein interaction surface, was obtained from solution NMR chemical shift perturbation data. The atomic level information reveals key intermolecular contacts identify...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Public Library of Science (PLoS)
2011-01-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC3080137?pdf=render |
| _version_ | 1818310474976985088 |
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| author | Ivano Bertini Soizic Chevance Rebecca Del Conte Daniela Lalli Paola Turano |
| author_facet | Ivano Bertini Soizic Chevance Rebecca Del Conte Daniela Lalli Paola Turano |
| author_sort | Ivano Bertini |
| collection | DOAJ |
| description | A structural model of the adduct between human cytochrome c and the human anti-apoptotic protein Bcl-x(L), which defines the protein-protein interaction surface, was obtained from solution NMR chemical shift perturbation data. The atomic level information reveals key intermolecular contacts identifying new potentially druggable areas on cytochrome c and Bcl-x(L). Involvement of residues on cytochrome c other than those in its complexes with electron transfer partners is apparent. Key differences in the contact area also exist between the Bcl-x(L) adduct with the Bak peptide and that with cytochrome c. The present model provides insights to the mechanism by which cytochrome c translocated to cytosol can be intercepted, so that the apoptosome is not assembled. |
| first_indexed | 2024-12-13T07:46:39Z |
| format | Article |
| id | doaj.art-5f40a10d621b40948b7099ffda8eb3f6 |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-13T07:46:39Z |
| publishDate | 2011-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-5f40a10d621b40948b7099ffda8eb3f62022-12-21T23:54:48ZengPublic Library of Science (PLoS)PLoS ONE1932-62032011-01-0164e1832910.1371/journal.pone.0018329The anti-apoptotic Bcl-x(L) protein, a new piece in the puzzle of cytochrome c interactome.Ivano BertiniSoizic ChevanceRebecca Del ConteDaniela LalliPaola TuranoA structural model of the adduct between human cytochrome c and the human anti-apoptotic protein Bcl-x(L), which defines the protein-protein interaction surface, was obtained from solution NMR chemical shift perturbation data. The atomic level information reveals key intermolecular contacts identifying new potentially druggable areas on cytochrome c and Bcl-x(L). Involvement of residues on cytochrome c other than those in its complexes with electron transfer partners is apparent. Key differences in the contact area also exist between the Bcl-x(L) adduct with the Bak peptide and that with cytochrome c. The present model provides insights to the mechanism by which cytochrome c translocated to cytosol can be intercepted, so that the apoptosome is not assembled.http://europepmc.org/articles/PMC3080137?pdf=render |
| spellingShingle | Ivano Bertini Soizic Chevance Rebecca Del Conte Daniela Lalli Paola Turano The anti-apoptotic Bcl-x(L) protein, a new piece in the puzzle of cytochrome c interactome. PLoS ONE |
| title | The anti-apoptotic Bcl-x(L) protein, a new piece in the puzzle of cytochrome c interactome. |
| title_full | The anti-apoptotic Bcl-x(L) protein, a new piece in the puzzle of cytochrome c interactome. |
| title_fullStr | The anti-apoptotic Bcl-x(L) protein, a new piece in the puzzle of cytochrome c interactome. |
| title_full_unstemmed | The anti-apoptotic Bcl-x(L) protein, a new piece in the puzzle of cytochrome c interactome. |
| title_short | The anti-apoptotic Bcl-x(L) protein, a new piece in the puzzle of cytochrome c interactome. |
| title_sort | anti apoptotic bcl x l protein a new piece in the puzzle of cytochrome c interactome |
| url | http://europepmc.org/articles/PMC3080137?pdf=render |
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