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首页> 美国卫生研究院文献>Biophysical Journal >Structural Preference for Changes in the Direction of the Ca2+-Induced Transition: A Study of the Regulatory Domain of Skeletal Troponin-C
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Structural Preference for Changes in the Direction of the Ca2+-Induced Transition: A Study of the Regulatory Domain of Skeletal Troponin-C

机译：Ca2 +诱导过渡方向变化的结构偏好：骨骼肌钙蛋白-C的调节域的研究。

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摘要

The determinants for specificity in the Ca2+-dependent response of the regulatory N-terminal domain of skeletal troponin-C are a combination of intrinsic and induced properties. We characterized computationally the intrinsic propensity of this domain for structural changes similar to those observed experimentally in the Ca2+-induced transition. The preference for such changes was assessed by comparing the structural effect of the harmonic and quasiharmonic vibrations specific for each Ca2+ occupancy with crystallographic data. Results show that only the Ca2+-saturated form of the protein features a slow vibrational motion preparatory for the transition. From the characteristics of this mode, we identified a molecular mechanism for transition, by which residues 42-51 of helix B and of the adjacent linker move toward helices (A, D), and bind to the surface used by the protein to interact with troponin-I. By obstructing the access of the target to hydrophobic residues important in the formation of the complex, helix B and the adjacent linker act as an autoinhibitory structural element. Specific properties of the methionines at the interaction surface were found to favor the binding of the autoinhibitory region. Located over hydrophobic residues critical for binding, the methionines are easily displaceable to increase the accessibility of these residues to molecular encounter.
机译：骨骼肌肌钙蛋白-C调节性N末端结构域的Ca 2 + 依赖性反应的特异性决定因素是内在和诱导性质的组合。我们通过计算表征了该结构域对结构变化的内在倾向，类似于在Ca 2 + 诱导的跃迁中实验观察到的倾向。通过比较每个Ca 2 + 占有率的谐波和准谐波振动的结构效应与晶体学数据来评估对这种变化的偏好。结果表明，只有Ca 2 + 饱和形式的蛋白质才能为过渡过程提供缓慢的振动运动。从这种模式的特征，我们确定了一种过渡的分子机制，通过该机制，螺旋B和相邻接头的残基42-51向着螺旋（A，D）移动，并与蛋白质用来与之相互作用的表面结合肌钙蛋白-I通过阻碍靶标进入在复合物形成过程中重要的疏水残基，螺旋B和相邻的接头可作为自抑制结构元件。发现在相互作用表面的蛋氨酸的特定性质有利于自抑制区域的结合。蛋氨酸位于对结合至关重要的疏水残基上，可轻松置换，以增加这些残基与分子接触的可及性。

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