http://www.cnr.it/ontology/cnr/individuo/prodotto/ID184709
Spectroscopic characterization of the complex between azurin and p53 transactivation domain (Contributo in atti di convegno)
- Type
- Label
- Spectroscopic characterization of the complex between azurin and p53 transactivation domain (Contributo in atti di convegno) (literal)
- Anno
- 2009-01-01T00:00:00+01:00 (literal)
- Alternative label
E. Gabellieri; M. Bucciantini; M. Stefani; P. Cioni (2009)
Spectroscopic characterization of the complex between azurin and p53 transactivation domain
in 7th EBSA European Biophysics Congress,, Genova, Italy, July 11-15 2009
(literal)
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- E. Gabellieri; M. Bucciantini; M. Stefani; P. Cioni (literal)
- Pagina inizio
- Pagina fine
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- 38, supplement 1 (literal)
- Rivista
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- Istituto di Biofisica, Consiglio Nazionale delle Ricerche, Pisa, Italy,
Department of Biochemical Sciences and Research Centre on the Molecular Basis of Neurodegeneration, University of Florence, Italy (literal)
- Titolo
- Spectroscopic characterization of the complex between azurin and p53 transactivation domain (literal)
- Abstract
- Recent reports have shown that the bacterial redox protein
azurin can enter into cancer cells and induce apoptosis by
stabilizing p53. The formation of a complex between the
two proteins has been demonstrated, but little is known
about binding features. For the first time, we show here that
azurin binds to the N-terminal region of p53 with a dissociation
constant in the 5-10 ?M range. Trp phosphorescence
lifetime measurements revealed conformational changes of
azurin induced by the interaction with p53(1-63). Acrylamide
quenching of Trp phosphorescence also indicated a
significant increase of the overall flexibility of azurin upon
binding to p53(1-63). No change of the fluorescence emission
of p53(1-63) was detected in the presence of azurin. The latter
finding suggests that W23 of p53 is not directly involved
in domain binding to azurin, indicating that the binding site
is distinct from that of MDM2. The present results may
assist the design of novel cancer treatments based on p53
stabilization by azurin. (literal)
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- Autore CNR
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