Departments of Chemistry, University of California, Davis, CA, 95616, USA.
Departments of Pharmacology, University of California, Davis, CA, 95616, USA.
Biomol NMR Assign. 2024 Dec;18(2):239-244. doi: 10.1007/s12104-024-10194-2. Epub 2024 Aug 29.
N-methyl-D-aspartate receptors (NMDARs) consist of glycine-binding GluN1 and glutamate-binding GluN2 subunits that form tetrameric ion channels. NMDARs in the brain are important for controlling neuronal excitability to promote synaptic plasticity. The cytoskeletal protein, α-actinin-1 (100 kDa, called ACTN1) binds to the cytosolic C0 domain of GluN1 (residues 841-865) that may play a role in the Ca-dependent desensitization of NMDAR channels. Mutations that disrupt NMDAR channel function are linked to Alzheimer's disease, depression, stroke, epilepsy, and schizophrenia. NMR chemical shift assignments are reported here for the C-terminal EF-hand domain of ACTN1 (residues 824-892, called ACTN_EF34) and ACTN_EF34 bound to the GluN1 C0 domain (BMRB numbers 52385 and 52386, respectively).
N-甲基-D-天冬氨酸受体（NMDARs）由甘氨酸结合的 GluN1 和谷氨酸结合的 GluN2 亚基组成，形成四聚体离子通道。大脑中的 NMDAR 对于控制神经元兴奋性以促进突触可塑性很重要。细胞骨架蛋白α-辅肌动蛋白-1（100 kDa，称为 ACTN1）与 GluN1 的胞质 C0 结构域（残基 841-865）结合，可能在 NMDAR 通道的 Ca2+依赖性脱敏中发挥作用。破坏 NMDAR 通道功能的突变与阿尔茨海默病、抑郁症、中风、癫痫和精神分裂症有关。本文报道了 ACTN1 的 C 端 EF 手结构域（残基 824-892，称为 ACTN_EF34）和与 GluN1 C0 结构域结合的 ACTN_EF34 的 NMR 化学位移赋值（BMRB 编号分别为 52385 和 52386）。
