The anti-apoptotic Bcl-x(L) protein, a new piece in the puzzle of cytochrome c interactome |
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Authors: | Bertini Ivano Chevance Soizic Del Conte Rebecca Lalli Daniela Turano Paola |
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Institution: | Magnetic Resonance Center (CERM), University of Florence, Sesto Fiorentino, Florence, Italy. bertini@cerm.unifi.it |
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Abstract: | 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. |
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