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 |
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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 |
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