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目的:通过理论方法建立M2蛋白酶的三维结构模型。方法:基于模板进行多重序列联配和结构联配建立M2蛋白酶的初始结构模型,对初始模型进行分子力学和分子动力学优化,用多种评价方法对所得结构进行合理评价。结果:得到了M2蛋白酶的三维结构模型,合理性评价结果表明该结构模型正确,M2蛋白酶的催化活性位点与天冬氨酸蛋白酶相似,区别在于与活性位点相邻的结构域的构象不同。结构保守区α碳原子叠合结果说明M2蛋白酶与其他天冬氨酸蛋白酶具有相同的生物进化来源。结论:M2蛋白酶的结构模型可以为进一步的分子生物学实验提供有益的参考,也可以此模型为基础进行数据库筛选和药物分子设计。
Objective: To establish a three-dimensional structural model of M2 protease by theoretical methods. Methods: The initial structural model of M2 protease was established based on the multiple sequence alignment and structural association. The initial model was optimized by molecular mechanics and molecular dynamics. The structure was evaluated by a variety of evaluation methods. Results: The three-dimensional structural model of M2 protease was obtained. The rational evaluation showed that the structural model was correct. The catalytic site of M2 protease was similar to that of aspartic protease except that the conformation of the domain adjacent to the active site was different . Convergence of the structurally conserved α-carbon atoms indicates that M2 protease has the same biological evolutionary origin as other aspartic proteases. CONCLUSION: The structural model of M2 protease can provide useful reference for further molecular biology experiments. It can also be used for database screening and drug molecule design based on this model.