Journal Article

FZJ-2014-02968

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Hepatitis C virus NS5A is able to competitively displace c-Myc from the Bin1 SH3 domain in vitro

Aladag, A.FZJ* ; Hoffmann, S.FZJ* ; Stoldt, M.FZJ* ; Bösing, C.FZJ* ; Willbold, D.FZJ* ; Schwarten, M. (Corresponding Author)FZJ*

2014
Wiley New York, NY [u.a.]

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Please use a persistent id in citations: doi:10.1002/psc.2618

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.

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Contributing Institute(s):

1. Strukturbiochemie (ICS-6)

Research Program(s):

1. 452 - Structural Biology (POF2-452) (POF2-452)

Appears in the scientific report 2014

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Database coverage:
; BIOSIS Previews ; Current Contents - Life Sciences ; JCR ; NCBI Molecular Biology Database ; Nationallizenz ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection

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