分子动力学模拟研究点突变(Met108→Leu108)对树胶醛糖结合蛋白与配体作用的影响  

Molecular Dynamics Simulation Study on the Effect of Mutant (Met108→Leu108) on Interactions Between Arabinose-binding Protein and Ligand

作　　者：冯献礼[1] 李卓[1] 赵熹[1] 于辉[2] 刘慧玲[1] 黄旭日[1] 

机构地区：[1]吉林大学理论化学研究所理论化学计算国家重点实验室,长春130021 [2]北华大学化学与生物学院,吉林132013

出　　处：《高等学校化学学报》2014年第2期338-343,共6页Chemical Journal of Chinese Universities

基　　金：国家'九七三'计划项目(批准号:2012CB932800);国家自然科学基金(批准号:21173097;21103066)资助~~

摘　　要：为了研究点突变(Met108→Leu108)对树胶醛糖结合蛋白(ABP)与配体结合能力的影响,对ABP、ABP结合树胶醛糖复合物及ABP结合半乳糖复合物以及它们各自的突变体分别进行60 ns的分子动力学模拟.模拟结果表明,108号残基突变前后,电子等排体的两个氨基酸残基,使蛋白与配体间的范德华相互作用发生明显变化,同时导致蛋白的内部运动也发生变化,进而影响蛋白与配体的相互作用.进一步分析表明,突变前后的蛋白构象变化都趋向于两个结构域张开,而与配体的结合可减缓张开程度.In order to understand the effect of the mutant（Met108→Leu108） of the arabinose-binding protein （ ABP） on the interactions between the protein and ligand, a series of 60 ns molecular dynamics simulations for the ABP, ABP bound ARA, ABP bound GAL and their mutants was performed, respectively. The results show that the mutation（Met108→Leu108） in ABP leads to the significant change of the van der Waals interac-tion between residue 108 and ligand, which further causes the changes of the protein＇s internal motion and in-teractions between the protein and ligand. The varieties in interaction between the protein and ligand make the two globular domains of wild-type and mutation-type of ABP gradually open and the ligand binding can control the open movement of the protein.

关 键 词：树胶醛糖结合蛋白 分子动力学 非极性相互作用 

分 类 号：O641.121[理学—物理化学]