Division of Molecular and Materials Simulation, State Key Laboratory of Organic-Inorganic Composites, Beijing University of Chemical Technology, Beijing 100029, People's Republic of China.
Sci Rep. 2013 Nov 20;3:3271. doi: 10.1038/srep03271.
We use a dissipative particle dynamic simulation to investigate the effects of shape complementarity on the protein-protein interactions. By monitoring different kinds of protein shape-complementarity modes, we gave a clear mechanism to reveal the role of the shape complementarity in the protein-protein interactions, i.e., when the two proteins with shape complementarity approach each other, the conformation of lipid chains between two proteins would be restricted significantly. The lipid molecules tend to leave the gap formed by two proteins to maximize the configuration entropy, and therefore yield an effective entropy-induced protein-protein attraction, which enhances the protein aggregation. In short, this work provides an insight into understanding the importance of the shape complementarity in the protein-protein interactions especially for protein aggregation and antibody-antigen complexes. Definitely, the shape complementarity is the third key factor affecting protein aggregation and complex, besides the electrostatic-complementarity and hydrophobic complementarity.
我们使用耗散粒子动力学模拟来研究形状互补性对蛋白质-蛋白质相互作用的影响。通过监测不同类型的蛋白质形状互补模式，我们给出了一个清晰的机制来揭示形状互补性在蛋白质-蛋白质相互作用中的作用，即当具有形状互补性的两个蛋白质相互接近时，它们之间的脂质链构象会受到显著限制。脂质分子倾向于离开两个蛋白质形成的间隙，以最大化构象熵，从而产生有效的熵诱导的蛋白质-蛋白质吸引力，这增强了蛋白质的聚集。总之，这项工作深入了解了形状互补性在蛋白质-蛋白质相互作用中的重要性，特别是对蛋白质聚集和抗体-抗原复合物的影响。可以肯定的是，除了静电互补性和疏水性互补性之外，形状互补性是影响蛋白质聚集和复合物的第三个关键因素。
