STUDYING INTERACTION SPECIFICITY BETWEEN GRIP & GLUR2

最近，离子通道已被证明与 细胞骨架蛋白，如PSD家族，包括PSD 93，95，97。 这些PSD蛋白都具有PDZ结构域，其负责 与所谓的XV基序在C-末端相互作用， 离子通道如K+通道和谷氨酸受体（例如，NR2A-D）。 另一种PDZ蛋白GRIP与另一种谷氨酸受体相互作用， GluR 2，其具有不同的C末端基序：ISEKI。 什么 决定了这种特殊性？ 我们现在正在分析 PSD 95 PDZ-XV复合物的结构。 我们也有兴趣 得到GRIP-ISEKI复合物的晶体结构。 我们将 能够准确地找出导致这种特定的 互动

Recently ion channels have been shown to interact with cytoskeleton proteins, like PSD families, including PSD93, 95, 97. These PSD proteins all have PDZ domains, which are responsible for interacting with the so-called XV motif at the very C-terminal of the ion channels like K+ channel and glutamate receptors (e.g., NR2A-D). Another PDZ protein, GRIP, interacts with another glutamate receptor, GluR2, which has a different C terminal motif: ISEKI. What determines this specificity? We are now analyzing the crystal structure of the PSD95 PDZ-XV complex. We are also interested in obtaining the crystal structure of GRIP-ISEKI complex. Thus we will be able to pinpoint the determinants responsible for this specific interaction.