磷脂酶A2及其复合物的分子动力学研究

本文运用分子动力学方法对磷脂酶A2的自由态以及有机小分子形成的复合物进行了研究．通过模型构建分子动力学模拟得到了磷脂酶A2与配体结合的模型，与磷脂酶A2的自由态相比，其口袋更为宽松，组成口袋的残基的结构趋于稳定，但催化残基的柔性变大．研究结果为药物分子设计提供了有用的信息．

Molecular Dynamic Study on Phospholipase A_2 and its Complex

Human Phospholipase A2 (PLA2) plays important role in the inflammation process. Inhibition of PLA2 could represent a possible point of therapeutic intervention in inflammation disorders. The crystal structure of PLA2 has been solved by Wery et al. In order to understand the interaction between the ligand and the enzyme, a known inhibitor was docked to the crystal structure of PLA2 to form a complex. Then, PLA2and its complex have been investigated by molecular dynamics simulation under the same conditions, using program CHARMM. On analysis of the complex model, we found an enlarged pocket with lower mobility compared to the uninhibited enzyme. The catalytic center is more flekible in complex, but the dynamic behavior of the remaining part in the enzyme is similar to that in the simulation. The analysis provides valuable information for drug design.