This title appears in the Scientific Report :
2014
Please use the identifier:
http://dx.doi.org/10.1002/psc.2618 in citations.
Hepatitis C virus NS5A is able to competitively displace c-Myc from the Bin1 SH3 domain in vitro
Hepatitis C virus NS5A is able to competitively displace c-Myc from the Bin1 SH3 domain in vitro
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 affin...
Saved in:
Personal Name(s): | Aladag, Amine |
---|---|
Hoffmann, Silke / Stoldt, Matthias / Bösing, Christina / Willbold, Dieter / Schwarten, Melanie (Corresponding Author) | |
Contributing Institute: |
Strukturbiochemie; ICS-6 |
Published in: | Journal of peptide science, 20 (2014) 5, S. 334 - 340 |
Imprint: |
New York, NY [u.a.]
Wiley
2014
|
PubMed ID: |
24616074 |
DOI: |
10.1002/psc.2618 |
Document Type: |
Journal Article |
Research Program: |
Structural Biology |
Publikationsportal JuSER |
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. |