Troponin structure and function: a view of recent progress
Troponin structure and function: a view of recent progress
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DOI：
10.1007/s10974-019-09513-1
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发表时间：
2020-03-01
影响因子：
2.7
通讯作者：
Zamora, Juan Eiros
中科院分区：
文献类型：
--
作者：
Marston, Steven;Zamora, Juan Eiros
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。揭示cTn的松弛和活性结构之间的差异，以及磷酸化后的构象变化，多年来一直是结构生物学家面临的挑战。在这里，我们回顾了目前的理解如何Ca 2+，磷酸化和致病突变影响肌钙蛋白的结构和动力学调节细丝的基础上，电子显微镜，X-射线衍射，核磁共振和分子动力学方法。
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.