SH2域与磷酸化多肽相互作用的连续溶剂模型研究

使用连续溶剂模型方法研究了SH2结构域与磷酸化多肽pYXXX(X为20种常见氨基酸残基中的任意一种)之间的相互作用.首先计算了已知的SH2域-磷酸化酪氨酸多肽复合物之间的结合能,理论计算的结果与实验测得的亲合能之间的相关系数为0.91,验证了理论模型的正确性.然后,用该模型方法计算了SH2域与pYXXX之间的结合能,分析了磷酸化酪氨酸多肽pYXXX中 1, 2, 3位置上残基对结合能的影响.结果表明 2, 3位置上残基的变化对结合能影响较大, 2位置上带负电的残基和 3位置上的疏水性残基有利于SH2域与pYXXX之间的相互作用,这与实验结果一致.

Continuum solvent model study of the interactions between SH2 domain and phosphotyrosine-containing peptides

Continuum solvent model is used to investigate the interactions between the SH2 domain and phosphotyrosine peptide pYXXX (X is any of the common 20 amino acid residues). Firstly, we calculated the binding energies of the SH2 domain and pY-containing peptides, which have been reported experimentally. The correlation coefficient between the theoretical values and the experimental ones is 0.91, demonstrating that our theoretical model is good enough to predict the interaction between SH2 and pY-containing peptides. Then, the same model is used to calculate the binding energies between the SH2 and pYXXX. Influence of the residues at the positions of 1, 2, and 3 on the binding energies is analyzed. The results show that the residues at positions of 2 and 3 have big impacts on the binding energies. The negatively charged residues at position of 2 and hydrophobic residues at position of 3 benefit the interactions between SH2 and pY-containing peptides, which is consistent very well with experiments.