Proteins are known to undergo structural changes upon binding to partner proteins. However, the prevalence, extent, location, and function of change in protein dynamics due to transient protein-protein interactions is not well documented. Here, we have analyzed a dataset of 58 protein-protein complexes of known three-dimensional structure and structures of their corresponding unbound forms to evaluate dynamics changes induced by binding. Fifty-five percent of cases showed significant dynamics change away from the interfaces. This change is not always accompanied by an observed structural change. Binding of protein partner is found to alter inter-residue communication within the tertiary structure in about 90% of cases. Also, residue motions accessible to proteins in unbound form were not always maintained in the bound form. Further analyses revealed functional roles for the distant site where dynamics change was observed. Overall, the results presented here strongly suggest that alteration of protein dynamics due to binding of a partner protein commonly occurs.

已知蛋白质在与伴侣蛋白质结合后会发生结构变化。然而，由于瞬时蛋白质-蛋白质相互作用而引起的蛋白质动力学变化的普遍性、程度、位置和功能没有得到很好的记录。在这里，我们分析了 58 种已知三维结构的蛋白质-蛋白质复合物及其相应未结合形式的结构的数据集，以评估结合引起的动力学变化。55% 的案例显示出远离界面的显着动态变化。这种变化并不总是伴随着观察到的结构变化。在大约 90% 的情况下，发现蛋白质伴侣的结合会改变三级结构内的残基间通讯。此外，未结合形式的蛋白质可接近的残基运动并不总是以结合形式保持。进一步的分析揭示了观察到动态变化的远程站点的功能作用。总体而言，此处呈现的结果强烈表明，由于伴侣蛋白的结合而导致的蛋白质动力学改变通常会发生。