Secondary structure and dynamics of micelle bound β- and γ-synuclein
Secondary structure and dynamics of micelle bound β- and γ-synuclein
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DOI：
10.1110/ps.051803606
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发表时间：
2006-05-01
期刊：
影响因子：
8
通讯作者：
Eliezer, D
中科院分区：
文献类型：
--
作者：
Sung, YH;Eliezer, D
我们使用溶液态核磁共振波谱来表征蛋白质β-和γ-突触核蛋白在其洗涤剂胶束结合构象中的二级结构和主链动力学。将这些结果与先前获得的帕金森病相关蛋白α-突触核蛋白的结果进行比较表明，三个同源突触核蛋白家族成员之间的结构差异与其一级氨基酸序列的变化直接相关。 β-突触核蛋白脂质结合域中的 11 个残基缺失会导致包含缺失位点的胶束结合螺旋结构的整个片段不稳定。 γ-突触核蛋白的酸性 C 末端尾部区域表现出广泛的序列差异，比其他两个家族成员的相应区域更加无序。观察到的结构差异可能介导三种蛋白质之间的功能变化，α-突触核蛋白和β-突触核蛋白之间的差异预计围绕它们的脂质相互作用，而γ-突触核蛋白功能的差异预计是由其独特的C端尾部介导的不同蛋白质-蛋白质相互作用造成的。
We have used solution state NMR spectroscopy to characterize the secondary structure and backbone dynamics of the proteins beta- and gamma-synuclein in their detergent micelle-bound conformations. Comparison of the results with those previously obtained for the Parkinson's disease-linked protein alpha-synuclein shows that structural differences between the three homologous synuclein family members are directly related to variations in their primary amino acid sequences. An 11-residue deletion in the lipid-binding domain of beta-synuclein leads to the destabilization of an entire segment of the micelle-bound helical structure containing the deletion site. The acidic C-terminal tail region of gamma-synuclein, which displays extensive sequence divergence, is more highly disordered than the corresponding regions in the other two family members. The observed structural differences are likely to mediate functional variations between the three proteins, with differences between alpha- and beta-synuclein expected to revolve around their lipid interactions, while differences in gamma-synuclein function are expected to result from different protein-protein interactions mediated by its unique C-terminal tail.