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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Crystal structure of monomeric human β-2-microglobulin reveals clues to its amyloidogenic properties
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Crystal structure of monomeric human β-2-microglobulin reveals clues to its amyloidogenic properties

机译:单体人β-2-微球蛋白的晶体结构揭示了其淀粉样蛋白生成特性的线索

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摘要

Dissociation of human β-2-microglobulin (β_2m) from the heavy chain of the class I HLA complex is a critical first step in the formation of amyloid fibrils from this protein. As a consequence of renal failure, the concentration of circulating monomeric β_2m increases, ultimately leading to deposition of the protein into amyloid fibrils and development of the disorder, dialysis-related amyloidosis. Here we present the crystal structure of a monomeric form of human β_2m determined at 1.8-A resolution that reveals remarkable structural changes relative to the HLA-bound protein.
机译:将人β-2-微球蛋白(β_2m)从I类HLA复合物的重链上解离是从该蛋白形成淀粉样蛋白原纤维的关键第一步。肾衰竭的结果是,循环性单体β_2m的浓度增加,最终导致蛋白质沉积到淀粉样蛋白原纤维中,并发展为与透析有关的淀粉样变性病。在这里,我们介绍了以1.8-A分辨率测定的人β_2m单体形式的晶体结构,该结构揭示了相对于HLA结合蛋白的显着结构变化。

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