基质金属蛋白酶S′<sub>1</sub>结合袋的分子动力学模拟

基质金属蛋白酶S′₁结合袋的分子动力学模拟

基金项目: 国家自然科学基金资助项目(No.81160383)；江西省科技支撑计划资助项目(No.2010BSA18500)

摘要: 研究基质金属蛋白酶(MMPs)的S′₁结合袋的分子动力学特点，并从分子水平上研究其对于设计特异性抑制剂的结构特点。对去除抑制剂后的MMP-7、MMP-2和MMP-3原酶进行长时间分子动力学模拟。结果显示，MMP-7和MMP-2的S′₁结合袋处于关闭状态，而MMP-3的S′₁结合袋处于半关闭状态，说明S′₁结合袋环区的柔性在结合抑制剂时发挥了重要作用。
- 基质金属蛋白酶 /
- 分子动力学 /
- S′₁结合袋
Abstract: To study the dynamic behavior of matrix metalloproteinases(MMPs)S′₁ binding pocket, and the structural properties relevant for the design of specific inhibitors at the molecular level, long-time molecular dynamics simulation of apo proteases of MMP-7, MMP-2 and MMP-3 were performed. It was found that the S′₁ binding pocket of MMP-7 and MMP-2 was closed, while S′₁ binding pocket of MMP-3 was semi-closed. Thus, the flexibility of S′₁ binding pocket loop region may play an important role in binding inhibitors.
- matrix metalloproteinase /
- molecular dynamics /
- S′₁ binding pocket