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蛋白质-蛋白质相互作用的作用机制对生命科学研究有着重要意义。目前已有的方法多偏向于氨基酸残基的偏好性研究,并没有给出对应的残基组合的空间信息,而这些空间信息对设计蛋白质-蛋白质相互作用至关重要。通过深入挖掘已有的蛋白质相互作用模式,并提炼残基相互作用对的偏好和相对位置信息,本文提出了一种全新的既能表征三元残基组合的偏好,又能给出三元残基组合对的空间信息的“三棱柱”模型。该模型主要从偏好因子、氨基酸组成和蛋白质二级结构分布等多个方面对三元残基组合对进行分析。此外,还将该模型应用于PD-1/PD-L2蛋白质的界面研究。通过分析PD-1/PD-L2蛋白质的界面残基组合对与预测残基组合对在组成和空间信息上的差异,给出了具体的残基突变建议,从而为蛋白质-蛋白质相互作用的设计提供了一种新的方法。
The mechanism of protein-protein interaction is of great importance to life science research. At present, the existing methods are mostly biased toward the study of amino acid residue preference and do not give the spatial information of the corresponding residue combinations, which is crucial for the design of protein-protein interactions. By digging out the existing patterns of protein interaction and refining the information about the preference and relative position of the residue interaction pair, a new preference for both the three-residue residue combination and the ternary residue Base combination of spatial information on the “Triangular prism” model. The model mainly analyzes the combinations of triad residues from the aspects of preference factor, amino acid composition and protein secondary structure distribution. In addition, the model was also applied to the interfacial study of PD-1 / PD-L2 proteins. By analyzing the differences in the compositional and spatial information of the combinations of the residues of the predicted PD-1 / PD-L2 proteins with the residues of the residues of the PD-1 / PD-L2 protein, specific residue mutation recommendations are given to design the protein-protein interaction Provide a new method.