与 NMDA 受体 GluN1（残基 841-865）胞质 C0 结构域结合的α-辅肌动蛋白 C 端 EF 手结构域的化学位移分配。
Chemical shift assignments of the α-actinin C-terminal EF-hand domain bound to a cytosolic C0 domain of GluN1 (residues 841-865) from the NMDA receptor.
机构信息
Departments of Chemistry, University of California, Davis, CA, 95616, USA.
Departments of Pharmacology, University of California, Davis, CA, 95616, USA.
出版信息
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）。
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