Department of Chemistry, University of California, Davis, CA, 95616, USA.
Biomol NMR Assign. 2023 Jun;17(1):61-65. doi: 10.1007/s12104-023-10121-x. Epub 2023 Feb 5.
Neuroplasticity and synaptic transmission in the brain are regulated by N-methyl-D-aspartate receptors (NMDARs) that consist of hetero-tetrameric combinations of the glycine-binding GluN1 and glutamate-binding GluN2 subunits. Calmodulin (CaM) binds to the cytosolic C0 domain of GluN1 (residues 841-865) that may play a role in the Ca-dependent inactivation (CDI) of NMDAR channel activity. Dysregulation of NMDARs are linked to various neurological disorders, including Alzheimer's disease, depression, stroke, epilepsy, and schizophrenia. Here, we report complete NMR chemical shift assignments of Ca-saturated CaM bound to the GluN1 C0 domain of the human NMDAR (BMRB no. 51715).
大脑中的神经可塑性和突触传递受 N-甲基-D-天冬氨酸受体 (NMDAR) 调节，该受体由结合甘氨酸的 GluN1 和结合谷氨酸的 GluN2 亚基的异四聚体组合组成。钙调蛋白 (CaM) 与 GluN1 的胞质 C0 结构域结合（残基 841-865），可能在 NMDAR 通道活性的 Ca 依赖性失活 (CDI) 中发挥作用。NMDAR 的失调与各种神经疾病有关，包括阿尔茨海默病、抑郁症、中风、癫痫和精神分裂症。在这里，我们报告了与人 NMDAR 的 GluN1 C0 结构域结合的饱和 Ca 的 CaM 的完整 NMR 化学位移分配（BMRB 编号 51715）。
