%0 Journal Article
%A Aladag, Amine
%A Hoffmann, Silke
%A Stoldt, Matthias
%A Bösing, Christina
%A Willbold, Dieter
%A Schwarten, Melanie
%T Hepatitis C virus NS5A is able to competitively displace c-Myc from the Bin1 SH3 domain in vitro
%J Journal of peptide science
%V 20
%N 5
%@ 1075-2617
%C New York, NY [u.a.]
%I Wiley
%M FZJ-2014-02968
%P 334 - 340
%D 2014
%X We studied the interaction of the SH3 domain of Bin1 with a 15-mer peptide of HCV NS5A and show its potency to competitively displace a 15-mer human c-Myc fragment, which is a physiological ligand of Bin1, using NMR spectroscopy. Fluorescence spectroscopy and ITC were employed to determine the affinity of Bin1 SH3 to NS5A(347–361), yielding a submicromolar affinity to NS5A. Our study compares the binding dynamics and affinities of the relevant regions for binding of c-Myc and NS5A to Bin1 SH3. The result gives further insights into the potential role of NS5A in Bin1-mediated apoptosis.Copyright © 2014 European Peptide Society and John Wiley & Sons, Ltd.
%F PUB:(DE-HGF)16
%9 Journal Article
%U <Go to ISI:>//WOS:000334824900004
%$ pmid:24616074
%R 10.1002/psc.2618
%U https://juser.fz-juelich.de/record/153336