TY  - JOUR
AU  - Aladag, Amine
AU  - Hoffmann, Silke
AU  - Stoldt, Matthias
AU  - Bösing, Christina
AU  - Willbold, Dieter
AU  - Schwarten, Melanie
TI  - Hepatitis C virus NS5A is able to competitively displace c-Myc from the Bin1 SH3 domain in vitro
JO  - Journal of peptide science
VL  - 20
IS  - 5
SN  - 1075-2617
CY  - New York, NY [u.a.]
PB  - Wiley
M1  - FZJ-2014-02968
SP  - 334 - 340
PY  - 2014
AB  - 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.
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000334824900004
C6  - pmid:24616074
DO  - DOI:10.1002/psc.2618
UR  - https://juser.fz-juelich.de/record/153336
ER  -