MBL2与MASPs家族蛋白质相互作用的生物信息学分析

Bioinformatics analysis of interaction between MBL2 and MASPs family proteins

目的:通过生物信息学方法对甘露糖结合凝集素2(MBL2)蛋白与甘露聚糖结合凝集素相关丝氨酸蛋白酶(MASPs)家族蛋白质的相互作用进行全面预测分析。方法:使用同源建模(Swiss-model)和折叠识别(Phyre2)分别来构建MBL2蛋白与MASPs家族蛋白质的结构,使用STRING数据库及ZDOCK3.02预测分析MBL2与MASP1、MASP2两个蛋白质的相互作用情况。结果: MBL2与MASP1和MASP2均存在直接相互作用,并且和COLEC11、COLEC10、FCN2、C4B等构成相互作用网络。MBL2与MASP1结合位点和MASP2的结合位点高度重叠。MBL2参与结合MASP1的残基,大部分(77%)也参与了与MASP2的结合,表明MBL2是通过同一个区域,分别与MASPs家族的蛋白质相互作用。结论: MBL2与MASPs家族蛋白质之间作用密切,从而可能在补体系统激活及机体免疫防御等方面发挥重要的作用。

Objective: The interaction between mannose-binding lectin 2(MBL2) protein and mannose-binding lectin-related serine proteases(MASPs) family proteins was comprehensively predicted and analyzed by bioinformatics. Methods: Homology modeling(Swiss-model) and fold recognition(Phyre 2) were used to construct the structure of MBL2 protein and MASPs family proteins respectively. STRING database and ZDOCK 3.02 were used to predict and analyze the interaction between MBL2 and MASP1 and MASP2 proteins. Results: MBL2 had direct interaction with MASP1 and MASP2, and formed interaction network with COLEEC11, COLEC10, FCN2 and C4 B. The binding sites of MBL2 and MASP1 and MASP2 overlap highly. MBL2 participates in the binding of MASP1 residues, and most of them(77%) are also involved in the binding of MASP2, suggesting that MBL2 interacts with the proteins of MASPs family through the same region. Conclusion: MBL2 and MASPs family proteins play an important role in complement system activation and immune defense.