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
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DOI：
10.1002/psc.2618
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发表时间：
2014-05-01
影响因子：
2.1
通讯作者：
Schwarten, Melanie
中科院分区：
文献类型：
--
作者：
Aladag, Amine;Hoffmann, Silke;Schwarten, Melanie
我们研究了BIN1的SH3结构域与丙型肝炎病毒NS5A的15聚体多肽的相互作用，并用核磁共振波谱显示了其竞争性地取代BIN1的生理配体c-Myc片段的效力。用荧光光谱和ITC测定了BIN1 SH3与NS5A(347-361)的亲和力，得到了与NS5A具有亚微摩尔亲和力的亲和力。我们的研究比较了c-Myc和NS5A与BIN1 SH3结合的相关区域的结合动力学和亲和力。这一结果进一步揭示了NS5A在BIN1介导的细胞凋亡中的潜在作用。版权所有(C)2014欧洲肽协会和John Wiley&Sons，Ltd.
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 (c) 2014 European Peptide Society and John Wiley & Sons, Ltd.