The structural basis of monoclonal antibody Alz50's selectivity for Alzheimer's disease pathology
The structural basis of monoclonal antibody Alz50's selectivity for Alzheimer's disease pathology
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DOI：
10.1074/jbc.271.51.32789
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发表时间：
1996-12-20
影响因子：
4.8
通讯作者：
Kuret, J
中科院分区：
文献类型：
--
作者：
Carmel, G;Mager, EM;Kuret, J
通过内部缺失诱变确定单克隆抗体Alz50识别的tau蛋白表位，并通过亲和测量定量。表位是不连续的，需要先前鉴定的n端片段和微管结合区才能有效结合Alz50。这些区域之间的相互作用与分子内反应机制一致，表明Alz50的结合取决于单个tau单体的构象。结果表明，tau蛋白在聚合成细丝时采用一种独特的构象，这种构象被Alz50选择性地识别。
The epitope on tau protein recognized by the monoclonal antibody Alz50 was defined through internal deletion mutagenesis and quantified by affinity measurements. The epitope is discontinuous and requires both a previously identified N-terminal segment and the microtubule binding region for efficient binding of Alz50. The interaction between these regions is consistent with an intramolecular reaction mechanism, suggesting that Alz50 binding depends on the conformation of individual tau monomers. The results suggest that tau adopts a distinct conformation when polymerized into filaments and that this conformation is recognized selectively by Alz50.