Inherent flexibility of calmodulin domains: A normal-mode analysis study
Inherent flexibility of calmodulin domains: A normal-mode analysis study
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DOI：
10.1021/jp026692q
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发表时间：
2002-10-24
影响因子：
3.3
通讯作者：
Caves, LSA
中科院分区：
文献类型：
--
作者：
Barton, NP;Verma, CS;Caves, LSA
两个钙调素（CaM）结构域的不同特征反映在不同的钙和靶相互作用的亲和力，与C-末端结构域通常显示出较高的亲和力。我们使用计算机模拟来研究这两个域的相对灵活性，以解决CaM域的不同属性和角色。我们使用了广泛的分子动力学模拟的各个域，以采样其构象空间。从这个样品的构象，我们进行了多个正常模式分析，计算振动和热力学性质。与N结构域相比，我们看到C结构域具有更高的内在灵活性。此外，在CaM-靶肽复合物的模拟中，C-结构域构象更好地保持其构象，并且具有比N-结构域更低的原子RMS波动。这些结果与观察到的钙调素结构域的作用分化。
The distinct character of the two calmodulin (CaM) domains is reflected in different calcium and target interaction affinities, with the C-terminal domain generally showing the higher affinities. We address the distinct properties and roles of the CaM domains by using computer simulations to examine the relative flexibility of the two domains. We used extensive molecular dynamics simulations of the individual domains to sample their conformational space. From this sample of conformations, we performed multiple normal-mode analyses to compute vibrational and thermodynamic properties. We see higher intrinsic flexibility of the C-domain compared with that of the N-domain. Furthermore, in a simulation of a CaM-target peptide complex, the C-domain conformation maintains its conformation better and has lower atomic RMS fluctuations than the N-domain. These results tie in with the observed differentiation of roles of the CaM domains.