摘要
目的验证重组人白细胞介素2(IL-2)-干扰素γ(IFN-γ)融合蛋白的生物活性。方法应用同源建模,构建了该融合蛋白的三维结构模型,并进行能量优化。结果通过与天然蛋白的三维结构比对,证明各组份在融合蛋白的折叠中,其骨架基本没改变;各组份活性部位并未被屏蔽,且可以与相应的受体对接,最终的结构可靠性评分较高,为其生物学活性提供了结构学依据。分子动力学模拟显示,融合蛋白的连接肽具有一定柔性,为融合蛋白两个组份分别行使各自功能提供了基础。结论重组人IL-2-IFN-γ融合蛋白具有天然的IL-2和IFN-γ的生物学活性。
Objective To validate the biological activity of fusion protein of interleukin-2 （IL-2） and interferon-γ （IFN-γ）. Methods By using the homology modeling, a three-dimensional structure model was established, and protein energy was optimized. Results Compared with natural IL-2 or IFN-γ, the structure of fusion protein was not changed, their active sites were not covered, and could be docked into their receptors preferably. Molecular dynamics simulations showed that linker peptide of fusion protein had much flexibility and laid the basis for respective biological functions of the two components, i.e. IL2 and IFN-γ. Conclusion Recombinant protein of IL-2 and IFN-γhas biological activities of natural IL-2 and IFN-γ.
出处
《华南国防医学杂志》
CAS
2010年第2期84-86,共3页
Military Medical Journal of South China
基金
国家"863"课题基金资助项目(2002AA2Z3317)
关键词
蛋白质结构预测
同源建模
分子对接
分子动力学模拟
融合蛋白
Protein structure prediction
Homology modeling
Molecular docking
Molecular dynamics simulations
Fusion protein
