底物结合对谷氨酰胺结合蛋白运动模式的影响

Effect of Substrate-binding on the Functional Motions of Glutamine Binding Protein

摘要: 为了研究底物谷氨酰胺（glutamine，Gln）的结合对谷氨酰胺结合蛋白（glutamine binding protein，GlnBP）运动特点的影响，采用分子对接方法研究了未结合Gln的GlnBP开放构象结构（GlnBP_O）与Gln的结合模式，获得了GlnBP_O-Gln复合物结构，然后用分子动力学（molecular dynamics，MD）模拟方法研究所获得的复合物的运动模式，并与GlnBP_O的运动模式相比较.结果表明：Gln特异性地结合在GlnBP_O的大结构域上，并且Gln的结合增加了GlnBP_O的闭合运动的速度和幅度.

Abstract: To study the effect of the binding of glutamine (Gln) on the motion characteristics of glutamine binding protein (GlnBP), molecular docking method was applied to ligand-free GlnBP in open conformation (GlnBP_O). The binding site of Gln on the large domain of GlnBP_O was characterized and the GlnBP_O-Gln complex was obtained. The results from the subsequent molecular dynamics (MD) simulations of the obtained GlnBP_O-Gln complex and GlnBP_O show that the binding of Gln on GlnBP_O enhances the close motion of GlnBP_O and forms the closed conformation eventually.