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.
Keywords:
Bin1; HCV; NMR; NS5A; SH3; protein-peptide interaction.
Copyright © 2014 European Peptide Society and John Wiley & Sons, Ltd.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adaptor Proteins, Signal Transducing / chemistry*
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Adaptor Proteins, Signal Transducing / metabolism*
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Apoptosis
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Binding, Competitive
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Calorimetry
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Magnetic Resonance Spectroscopy
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Models, Molecular
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Nuclear Proteins / chemistry*
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Nuclear Proteins / metabolism*
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Proto-Oncogene Proteins c-myc / chemistry
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Proto-Oncogene Proteins c-myc / metabolism*
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Spectrometry, Fluorescence
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Tumor Suppressor Proteins / chemistry*
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Tumor Suppressor Proteins / metabolism*
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Viral Nonstructural Proteins / chemistry
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Viral Nonstructural Proteins / metabolism*
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src Homology Domains*
Substances
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Adaptor Proteins, Signal Transducing
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BIN1 protein, human
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Nuclear Proteins
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Proto-Oncogene Proteins c-myc
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Tumor Suppressor Proteins
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Viral Nonstructural Proteins
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NS-5 protein, hepatitis C virus