Department of Medical Life Science, Graduate School of Medical Life Science, Yokohama City University, Suehiro-cho, Tsurumi-ku, Yokohama, 230-0045, Japan.
Department of Biology, University of Virginia, Charlottesville, VA, 22904, USA.
Sci Rep. 2019 Jul 23;9(1):10688. doi: 10.1038/s41598-019-47063-1.
Calmodulin is a calcium binding protein with two lobes, N-lobe and C-lobe, which evolved from duplication and fusion of a single precursor lobe of a pair of EF-hand. These two lobes of calmodulin show subtle differences in calcium binding and target recognition; these are important for the functions of calmodulin. Since the structures, especially main chain conformations, of two EF-lobes in holo-form are quite similar; this is a good example to evaluate the effect of side chains for structural dynamics. We analyzed the structure of calmodulin using molecular dynamics and found differences in conformational ensembles between N- and C-lobes. We also showed the mutant structures created by homology modeling could reproduce the difference of dynamic motion between N- and C-lobes.
钙调蛋白是一种钙结合蛋白，具有两个结构域，N 结构域和 C 结构域，它是由一对 EF 手结构域中单个前体结构域的复制和融合演化而来的。钙调蛋白的这两个结构域在钙结合和靶标识别方面表现出细微的差异；这些对钙调蛋白的功能很重要。由于在完整形式下，两个 EF 结构域的结构，特别是主链构象，非常相似；这是评估侧链对结构动力学影响的一个很好的例子。我们使用分子动力学分析了钙调蛋白的结构，发现 N 结构域和 C 结构域的构象集合之间存在差异。我们还表明，通过同源建模创建的突变体结构可以再现 N 结构域和 C 结构域之间动态运动的差异。
