The anti-apoptotic Bcl-xl protein, a new piece in the puzzle of cytochrome c interactome

Ivano Bertini, Soizic Chevance, Rebecca Del Conte, Daniela Lalli, Paola Turano

Risultato della ricerca: Contributo su rivistaArticolo in rivistapeer review

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 originaleInglese
Numero di articoloe18329
RivistaPLoS ONE
Volume6
Numero di pubblicazione4
DOI
Stato di pubblicazionePubblicato - 2011
Pubblicato esternamente

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