The anti-apoptotic Bcl-x(L) protein, a new piece in the puzzle of cytochrome c interactome

Autor: Paola Turano, Soizic Chevance, Daniela Lalli, Ivano Bertini, Rebecca Del Conte
Přispěvatelé: Magnet Resonance Center (CERM), Università degli Studi di Firenze = University of Florence [Firenze] (UNIFI), Institut des Sciences Chimiques de Rennes (ISCR), Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-Institut National des Sciences Appliquées - Rennes (INSA Rennes), Institut National des Sciences Appliquées (INSA)-Université de Rennes (UNIV-RENNES)-Institut National des Sciences Appliquées (INSA)-Ecole Nationale Supérieure de Chimie de Rennes (ENSCR)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Università degli Studi di Firenze = University of Florence (UniFI), Université de Rennes (UR)-Institut National des Sciences Appliquées - Rennes (INSA Rennes), Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Ecole Nationale Supérieure de Chimie de Rennes (ENSCR)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)
Jazyk: angličtina
Rok vydání: 2011
Předmět:
Macromolecular Assemblies
Models
Molecular

Protein Structure
Cytochrome
Static Electricity
Biophysics
bcl-X Protein
lcsh:Medicine
Apoptosis
Bcl-xL
Plasma protein binding
Biochemistry
Protein–protein interaction
Electron Transport
03 medical and health sciences
chemistry.chemical_compound
0302 clinical medicine
Macromolecular Structure Analysis
Humans
lcsh:Science
Biology
Bioinorganic Chemistry
Nuclear Magnetic Resonance
Biomolecular

Heme
Macromolecular Complex Analysis
030304 developmental biology
0303 health sciences
Multidisciplinary
biology
Chemistry
Systems Biology
Cytochrome c
lcsh:R
Computational Biology
Cytochromes c
[CHIM.MATE]Chemical Sciences/Material chemistry
Electron transport chain
030220 oncology & carcinogenesis
biology.protein
lcsh:Q
Apoptosome
cytochorme c
BcL-xL
apoptosis
antiapoptotic proteins
protein-protein interactions
NMR

Research Article
Protein Binding
Zdroj: PLoS ONE, Vol 6, Iss 4, p e18329 (2011)
PLoS ONE
PLoS ONE, Public Library of Science, 2011, 6 (4), pp.e18329. ⟨10.1371/journal.pone.0018329⟩
PLoS ONE, 2011, 6 (4), pp.e18329. ⟨10.1371/journal.pone.0018329⟩
ISSN: 1932-6203
DOI: 10.1371/journal.pone.0018329⟩
Popis: International audience; 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.
Databáze: OpenAIRE