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Updated: May 2, 2026

A Protocol for Analyzing Hepatitis C Virus Replication
Published on: June 26, 2014
Hepatitis C virus NS5A is able to competitively displace c-Myc from the Bin1 SH3 domain in vitro
Amine Aladag1, Silke Hoffmann, Matthias Stoldt
1Institut für Physikalische Biologie, Heinrich-Heine-Universität, 40225, Düsseldorf, Germany; Institute of Complex Systems (ICS-6) Structural Biochemistry, Forschungszentrum Jülich, 52425, Jülich, Germany.
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.
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