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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >X-ray crystallographic studies of two transthyretin variants: further insights into amyloidogenesis
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X-ray crystallographic studies of two transthyretin variants: further insights into amyloidogenesis

机译：x射线晶体的两个研究转体基因变体:进一步的见解amyloidogenesis

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摘要

Transthyretin (TTR) is a homotetrameric plasma protein that, as a result of a set of not yet fully characterized conformational changes, forms fibrillar aggregates that are the major protein component of amyloid deposits. More than 80 mutations associated with TTR amyloid deposition have been described in the literature. X-ray crystallography was used to elucidate the three-dimensional structure of two important TTR variants: TTR Y78F, an amyloidogenic protein, and TTR R104H, which is associated with a protective effect over the amyloidogenic V30M mutation. The structures of those two TTR variants have been determined in space group P2(1)2(1)2 to 1.55 and 1.60 Angstrom resolution, respectively, using molecular-replacement techniques. Detailed analysis of the protein model for TTR Y78F indicates a destabilization of the contacts between the a-helix and AB loop and the body of the molecule, intimately related to the amyloidogenic nature; contrastingly, in the TTR R104H variant new contacts involving the N-terminal region and His104 are clearly antagonists of amyloid formation.
机译：转体基因(竞技场队伍)是一个homotetrameric等离子体蛋白质,由于一组没有完全构象变化特征,形式纤维总量的主要蛋白质组件的淀粉样蛋白沉积。突变与淀粉样沉积竞技场队伍有关在文献中均有描述。晶体学是用来阐明三维结构的两个重要的竞技场队伍变体:Y78F竞技场队伍,amyloidogenic蛋白质,R104H竞技场队伍,保护效应在amyloidogenic V30M突变。这两个竞技场队伍结构变异确定空间群P2(1)和2(1)2到1.551.60埃分辨率,分别使用molecular-replacement技术。分析蛋白质的模型Y78F竞技场队伍显示不稳定的联系一个螺旋和AB之间的循环的身体分子,密切相关amyloidogenic自然;新联系人涉及R104H变体氨基端地区His104明显对手的淀粉样蛋白的形成。

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