α-突触核蛋白的结构特点及其功能  

The structural features and functions of α-synuclein

作　　者：张振伟[1] 张建鹏[1] 周婷婷[1] 冯伟华[1] 焦炳华[1] 

机构地区：[1]第二军医大学基础部生物化学与分子生物学教研室,上海200433

出　　处：《生命的化学》2010年第1期114-118,共5页Chemistry of Life

基　　金：上海市自然科学基金(09ZR1439600)资助

摘　　要：神经元胞浆内嗜酸性包涵体——Lewy体的出现是帕金森病(Parkinson’s disease,PD)的典型病理学特征,而α-突触核蛋白(α-synuclein)是纤维样Lewy体的主要成分。随着研究深入,越来越多的证据表明:α-突触核蛋白纤维性聚集体的产生是PD发病的一个关键环节。病理条件下,由于α-突触核蛋白的结构改变,导致错误折叠,继而纤维化,最终形成纤维性聚集体,这一过程在PD研究中日趋展现出其重要性。α-突触核蛋白结构中,N端、C端、NAC(non-amyloid component)区等区域具有各自特定的结构及功能,在其聚集体产生过程中各司其职。本文就近年来对α-突触核蛋白分子结构及其相应功能的研究进行综述,希望通过深入的综合分析,为寻找α-突触核蛋白结构中潜在的疾病治疗靶标提供理论依据。Aggregation of α-synuclein, the major component of Lewy bodies, is thought to be a key event in the pathogenesis of Parkinson＇s disease. Under the pathological condition, conformational changes of α-synuclein protein results in its misfolding and abnormal fibrillar aggregation. Physiologically, natively unfolded α-synuclein consists of three distinct regions, including an N-terminal region, a hydrophobic center domain （non-amyloid component, NAC） and a C-terminus region, which all play important roles in the process of its aggregation. In hope of providing some theoretical evidence of finding potential therapeu- tic target, this review focuses on studies of the structural features and their functions of α-synuclein in recent years.

关 键 词：Α-突触核蛋白 结构 功能 

分 类 号：R742.5[医药卫生—神经病学与精神病学]