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Investigation of a Direct Interaction between miR4749 and the Tumor Suppressor p53 by Fluorescence, FRET and Molecular Modeling

Biomolecules. 2020; 
Bizzarri AR, Cannistraro S.
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Molecular Biology Reagents … 2 Materials and Methods 21 Materials Recombinant human DNA binding domain (DBD) of p53, formed by the 94-300 residues, including a single Tryptophan (Trp 146), was purchased from Genscript (Piscataway, NJ, USA) … Get A Quote

摘要

The interactions between the DNA binding domain (DBD) of the tumor suppressor p53 and miR4749, characterized by a high sequence similarity with the DNA Response Element (RE) of p53, was investigated by fluorescence spectroscopy combined with computational modeling and docking. Fluorescence quenching experiments witnessed the formation of a specific complex between DBD and miR4749 with an affinity of about 105 M. Förster Resonance Energy Transfer (FRET) allowed us to measure a distance of 3.9 ± 0.3 nm, between the lone tryptophan of DBD and an acceptor dye suitably bound to miR4749. Such information, combined with a computational modeling approach, allowed us to predict possible structures for the DBD-miR4749 ... More

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