Abstract
A structural model of the adduct between human cytochrome c and the human anti-apoptotic protein Bcl-xL, 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-xL. 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-xL 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.
Lingua originale | Inglese |
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Numero di articolo | e18329 |
Rivista | PLoS ONE |
Volume | 6 |
Numero di pubblicazione | 4 |
DOI | |
Stato di pubblicazione | Pubblicato - 2011 |
Pubblicato esternamente | Sì |