摘要
对imatinib两种典型复合物晶体结构imatinib-Abl与imatinib-c-Kit进行比对分析,并利用MM/PBSA方法计算imatinib与Abl、c-Kit、c-Src、p38及Syk等激酶的结合自由能.计算结果表明,imatinib与上述激酶结合时,范德华作用对结合自由能有主要贡献;其中,imatinib与激酶c-Kit结合自由能最低;imatinib与非活性构象激酶的结合自由能明显低于与活性构象激酶的结合自由能.
The crystal structures of imatinib-Abl and imatinib-c-Kit complexes were compared, and the MM/PBSA method was used to calculate the binding free energies of imatinib to kinases such as Abl, e-Kit, Sre and p38. The results indicate that the van der Waals interactions make major contributions to the binding free energies of imatinib. The complex imatinib-c-kit has the lowest free energy among the six complexes. The results also show that the free energies of imatinib binding to inactive kinases are obviously lower than those active kinases.
出处
《西华师范大学学报（自然科学版）》
2012年第3期290-293,303,共5页
Journal of China West Normal University(Natural Sciences)
基金
四川省教育厅自然科学重点项目(11ZA294)
西华师范大学科研启动基金资助项目(No:10B006)
