CONFORMATIONAL CHANGE OF GLUR2 UPON INTERACTION W/ GRIP & NSF

最近的生化数据显示，C末端的尾巴(50个氨基酸 酸)离子通道GluR2与接头的PDZ结构域相互作用 蛋白GRIP和ATPase NSF相互排他性。缺失突变体 研究表明，GRIP和NSF绑定到两个不同的伸展 GluR2 C端尾(分别为7个和10个氨基酸)。这些是如何 相互遮挡的相互作用正在调查中。一股水流 模型表明了一种屏蔽效应：一次互动的主题将 一旦其他母题已经参与互动，就会被屏蔽。 我们正试图获得并分析该化合物的晶体结构 GluR2，GRIP和GluR2，NSF复合体，将使我们能够精确定位 图案屏蔽效果的结构基础。

Recent biochemistry data shows that the C terminal tail (50 amino acids) of ion channel GluR2 interacts with the PDZ domain of adaptor protein GRIP and ATPase NSF mutually exclusively. Deletion mutants studies suggest that GRIP and NSF binds to two different stretches of GluR2 C-terminal tail (7 and 10 amino acids), respectively. How these interactions occlude each other is under investigation. A current model suggests a shielding effect: the motif for one interaction will be shielded once the other motif engages in the interaction already. We are trying to obtain and analyze the crystal structure of the GluR2, GRIP and GluR2, NSF complexes which will allow us to pinpoint structural bases for the motif shielding effect.