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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Domain swapping is a consequence of minimal frustration
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Domain swapping is a consequence of minimal frustration

机译：域交换是最小程度的挫败的结果

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摘要

The same energy landscape principles associated with the folding of proteins into their monomeric conformations should also describe how these proteins oligomerize into domain-swapped conformations. We tested this hypothesis by using a simplified model for the epidermal growth factor receptor pathway substrate 8 src homology 3 domain protein, both of whose monomeric and domain-swapped structures have been solved. The model, which we call the symmetrized Go-type model, incorporates only information regarding the monomeric conformation in an energy function for the dinner to predict the domain-swapped conformation. A striking preference for the correct domain-swapped structure was observed, indicating that overall monomer topology is a main determinant of the structure of domain-swapped dimers. Furthermore, we explore the free energy surface for domain swapping by using our model to characterize the mechanism of oligomerization.
机译：与蛋白质折叠成单体构象有关的相同能量构图原理也应描述这些蛋白质如何寡聚为域交换构象。我们使用表皮生长因子受体途径底物8 src同源性3域蛋白的简化模型测试了该假设，该蛋白的单体结构和结构域交换结构均已解决。该模型称为对称Go型模型，该模型仅在晚餐的能量函数中包含有关单体构象的信息，以预测域交换构象。观察到对正确的域交换结构的强烈偏好，表明整体单体拓扑结构是域交换二聚体结构的主要决定因素。此外，我们通过使用我们的模型来表征低聚机理来探索用于域交换的自由能表面。

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