高级检索

基质金属蛋白酶S′1结合袋的分子动力学模拟

Molecular dynamics simulation of matrix metalloproteinases S′1 binding pocket

  • 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。

     

    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.

     

/

返回文章
返回