The molecular mechanism by which Ca²⁺ binding and phosphorylation regulate muscle contraction through Troponin is not yet fully understood. Revealing the differences between the relaxed and active structure of cTn, as well as the conformational changes that follow phosphorylation has remained a challenge for structural biologists over the years. Here we review the current understanding of how Ca²⁺, phosphorylation and disease-causing mutations affect the structure and dynamics of troponin to regulate the thin filament based on electron microscopy, X-ray diffraction, NMR and molecular dynamics methodologies.

中文翻译：

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肌钙蛋白的结构和功能：近期进展的看法。

Ca ²⁺结合和磷酸化通过肌钙蛋白调节肌肉收缩的分子机制尚未完全了解。多年来，揭示cTn的松弛结构与活性结构之间的差异以及磷酸化后的构象变化一直是结构生物学家的挑战。在这里，我们基于电子显微镜，X射线衍射，NMR和分子动力学方法，回顾当前对Ca ²⁺，磷酸化和致病突变如何影响肌钙蛋白的结构和动力学以调节细丝的认识。