Selective protein-protein interactions driven by a phenylalanine interface
Selective protein-protein interactions driven by a phenylalanine interface
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DOI：
10.1021/ja055494k
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发表时间：
2006-01-11
影响因子：
15
通讯作者：
Kumar, K
中科院分区：
文献类型：
--
作者：
Yoder, NC;Kumar, K
高度特异性的蛋白质-蛋白质界面因其在干扰或询问细胞信号和控制网络中的潜在效用而成为大量研究的主题。我们报告说，卷曲螺旋序列装饰苯丙氨酸核心残基折叠成稳定的α-螺旋束，这些自我排序从类似的肽组件与脂肪族核心侧链。对于衍生自30个残基的单体肽的自组装系综，特异性的Δ G为~ 1.5 kcal/mol，与早期的自分选卷曲螺旋系统相当。有趣的是，虽然这种界面是由典型的氨基酸构建的，但它似乎并没有在天然蛋白质中被利用。
Highly specific protein-protein interfaces have been the subject of considerable study for their potential utility in disrupting or interrogating cellular signaling and control networks. We report that coiled-coil sequences decorated with phenylalanine core residues fold into stable a-helical bundles and that these self-sort from similar peptide assemblies with aliphatic core side chains. For self-assembled ensembles derived from 30-residue monomeric peptides, the Delta G of specificity is -1.5 kcal/mol, comparable with earlier self-sorting coiled-coil systems. Intriguingly, although this interface is constructed from canonical amino acids, it does not appear to have been exploited in native proteins.