NMR assignment of the spinophilin PDZ domain (493-602).
NMR assignment of the spinophilin PDZ domain (493-602).
复制标题
亲旋蛋白 PDZ 结构域 (493-602) 的 NMR 归属。
DOI：
10.1007/s10858-006-0006-x
复制
发表时间：
2006
影响因子：
2.7
通讯作者：
Peti,Wolfgang
中科院分区：
文献类型：
--
作者：
Kelker,MatthewS;Peti,Wolfgang
多结构域支架蛋白亲棘素（艾伦等人，1997）是突触后密度中的关键调节和靶向蛋白之一。它将蛋白磷酸酶1（PP 1）靶向其细胞作用点。这种靶向作用负责PP 1介导的对谷氨酸能AMPA/NMDA通道活性的调节（Greengard，2001）。基于一级序列比较，我们鉴定了Spinophilin（493-602）的PDZ结构域。为了深入了解结构特征并筛选可能的相互作用伙伴，我们开始了NMR研究。我们使用13 C，15 N标记的Spinophilin 493 -602进行异源2D和3D NMR实验，用于化学位移归属。Spinophilin 493 -602的1H、13 C和15 N归属基本上是完整的（超过97%的碳和95%的质子），除了G1、H2、R81、R88和E108的氮和酰胺质子，M3、24、30和90的eCH 3，以及G2的Ha 2/3。还缺少芳族碳化学位移和F6、75和89的Hf。登录号为6927的BMRB存款。
The multi-domain scaffolding protein spinophilin (Allen et al., 1997) is one of the key regulator and targeting proteins in the post synaptic density. It targets Protein Phosphatase 1 (PP1) to its cellular point of action. This targeting is responsible for the PP1-mediated regulation of glutamatergic AMPA/NMDA channel activity (Greengard, 2001). Based on primary sequence comparison we identified the PDZ domain of Spinophilin (493–602). To gain insight into the structural features and to screen for possible interaction partners we initiated an NMR investigation. We used heteronuclear 2D and 3D NMR experiments, using 13C, 15N labeled Spinophilin493–602, for the chemical shift assignment. The 1H, 13C and 15N assignments of Spinophilin493–602 are essentially complete (more than 97% carbon and 95% proton) with the exceptions being the nitrogen and amide proton of G1, H2, R81, R88 and E108, the e CH3 of M3, 24, 30 and 90, and the Ha2/3 of G2. Also missing are the aromatic carbon chemical shifts and the Hf of F6, 75 and 89. BMRB deposit with accession number 6927.