Molecular basis of the head‐to‐tail assembly of giant muscle proteins obscurin‐like 1 and titin
Molecular basis of the head‐to‐tail assembly of giant muscle proteins obscurin‐like 1 and titin
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DOI：
10.1038/embor.2010.65
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发表时间：
2010-07
期刊：
影响因子：
7.7
通讯作者：
F. Sauer;J. Vahokoski;Young-Hwa Song;M. Wilmanns
中科院分区：
文献类型：
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作者：
F. Sauer;J. Vahokoski;Young-Hwa Song;M. Wilmanns
肌肉肌节中的大纤维蛋白包含许多免疫球蛋白样结构域，这些结构域为自组装和与异源蛋白伴侣的相互作用提供了分子平台。我们已经通过X射线晶体学揭示了titin的羧基端和obscurin - like - 1的氨基端头尾相互作用的分子基础。二元复合物由平行的分子间β -薄片形成，在肌丝蛋白中呈现一种新的免疫球蛋白样结构域介导的组装机制。互补结合数据表明，组装是熵驱动的，而不是由特定的极性相互作用主导的数据。观察到的组装导致两种丝蛋白呈V形拉链状排列。
Large filament proteins in muscle sarcomeres comprise many immunoglobulin‐like domains that provide a molecular platform for self‐assembly and interactions with heterologous protein partners. We have unravelled the molecular basis for the head‐to‐tail interaction of the carboxyl terminus of titin and the amino‐terminus of obscurin‐like‐1 by X‐ray crystallography. The binary complex is formed by a parallel intermolecular β‐sheet that presents a novel immunoglobulin‐like domain‐mediated assembly mechanism in muscle filament proteins. Complementary binding data show that the assembly is entropy‐driven rather than dominated data by specific polar interactions. The assembly observed leads to a V‐shaped zipper‐like arrangement of the two filament proteins.