CONFORMATIONAL CHANGE OF GLUR2 UPON INTERACTION W/ GRIP & NSF

最近的生物化学数据表明，C末端尾（50个氨基酸） 离子通道GluR 2的氨基酸）与衔接子的PDZ结构域相互作用 蛋白质GRIP和ATP酶NSF互斥。 缺失突变体 研究表明，GRIP和NSF结合到两个不同的延伸， GluR 2 C-末端尾（7和10个氨基酸）。 如何将这些 相互作用相互遮挡正在调查中。 电流 模型提出了一种屏蔽效应：一种相互作用的基序将 一旦另一个主题已经参与到互动中，就会被屏蔽。 我们正试图获得和分析的晶体结构的 GluR 2，GRIP和GluR 2，NSF复合物，这将使我们能够确定 图案屏蔽效应的结构基础。

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.