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@ARTICLE{Aladag:153336,
author = {Aladag, Amine and Hoffmann, Silke and Stoldt, Matthias and
Bösing, Christina and Willbold, Dieter and Schwarten,
Melanie},
title = {{H}epatitis {C} virus {NS}5{A} is able to competitively
displace c-{M}yc from the {B}in1 {SH}3 domain in vitro},
journal = {Journal of peptide science},
volume = {20},
number = {5},
issn = {1075-2617},
address = {New York, NY [u.a.]},
publisher = {Wiley},
reportid = {FZJ-2014-02968},
pages = {334 - 340},
year = {2014},
abstract = {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.},
cin = {ICS-6},
ddc = {570},
cid = {I:(DE-Juel1)ICS-6-20110106},
pnm = {452 - Structural Biology (POF2-452)},
pid = {G:(DE-HGF)POF2-452},
typ = {PUB:(DE-HGF)16},
UT = {WOS:000334824900004},
pubmed = {pmid:24616074},
doi = {10.1002/psc.2618},
url = {https://juser.fz-juelich.de/record/153336},
}