THE PRIMARY STRUCTURE AND HETEROGENEITY OF TAU-PROTEIN FROM MOUSE-BRAIN
THE PRIMARY STRUCTURE AND HETEROGENEITY OF TAU-PROTEIN FROM MOUSE-BRAIN
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DOI：
10.1126/science.3122323
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发表时间：
1988-01-15
期刊：
影响因子：
56.9
通讯作者：
KIRSCHNER, M
中科院分区：
文献类型：
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作者：
LEE, G;COWAN, N;KIRSCHNER, M
Tau蛋白是微管结合蛋白的一个家族，分子量不均匀，在神经突生长过程中被诱导，并在阿尔茨海默病的神经元缠结中显著发现。从互补DNA克隆中确定了小鼠脑中两种形式的tau蛋白的预测氨基酸序列。这些形式在它们的氨基末端序列中是相同的，但在它们的羧基末端结构域中不同。这两种蛋白质都含有可能是微管蛋白结合位点的重复序列。该序列表明tau是一种伸长的分子，没有广泛的α-螺旋或β-片域这些互补的DNA应该能够研究tau蛋白的各种功能结构域，并研究正常和病理状态下的tau蛋白表达。
Tau protein is a family of microtubule binding proteins, heterogeneous in molecular weight, that are induced during neurite outgrowth and are found prominently in neurofibrillary tangles in Alzheimer''s disease. The predicted amino acid sequences of two forms of tau protein from mouse brain were determined from complementary DNA clones. These forms are identical in their amino-terminal sequences but differ in their carboxyl-terminal domains. Both proteins contain repeated sequences that may be tubulin binding sites. The sequence suggests that tau is an elongated molecule with no extensive .alpha.-helical or .beta.-sheet domains. These complementary DNAs should enable the study of various functional domains of tau and the study of tau expression in normal and pathological states.