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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
2011-5-2
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pubmed:abstractText |
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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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/21533126-10631615,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/21533126-9735050
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:issn |
1932-6203
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
6
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
e18329
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pubmed:meshHeading |
pubmed-meshheading:21533126-Apoptosis,
pubmed-meshheading:21533126-Cytochromes c,
pubmed-meshheading:21533126-Electron Transport,
pubmed-meshheading:21533126-Humans,
pubmed-meshheading:21533126-Models, Molecular,
pubmed-meshheading:21533126-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:21533126-Protein Binding,
pubmed-meshheading:21533126-Static Electricity,
pubmed-meshheading:21533126-bcl-X Protein
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pubmed:year |
2011
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pubmed:articleTitle |
The anti-apoptotic Bcl-x(L) protein, a new piece in the puzzle of cytochrome c interactome.
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pubmed:affiliation |
Magnetic Resonance Center (CERM), University of Florence, Sesto Fiorentino, Florence, Italy. bertini@cerm.unifi.it
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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