NMDA受体结合GluN2A胞质结构域(残基1004-1024)的钙调蛋白的化学移位配位

IF 0.8 4区生物学 Q4 BIOPHYSICS

Biomolecular NMR Assignments Pub Date : 2023-04-07 DOI:10.1007/s12104-023-10125-7

Aritra Bej, James B. Ames

{"title":"NMDA受体结合GluN2A胞质结构域(残基1004-1024)的钙调蛋白的化学移位配位","authors":"Aritra Bej, James B. Ames","doi":"10.1007/s12104-023-10125-7","DOIUrl":null,"url":null,"abstract":"<div><p>N-methyl-D-aspartate receptors (NMDARs) consist of glycine-binding GluN1 and glutamate-binding GluN2 subunits that form tetrameric ion channels. NMDARs in the neuronal post-synaptic membrane are important for controlling neuroplasticity and synaptic transmission in the brain. Calmodulin (CaM) binds to the cytosolic C0 domains of both GluN1 (residues 841–865) and GluN2 (residues 1004–1024) that may play a role in the Ca<sup>2+</sup>-dependent desensitization of NMDAR channels. Mutations that disrupt Ca<sup>2+</sup>-dependent desensitization of NMDARs are linked to Alzheimer’s disease, depression, stroke, epilepsy, and schizophrenia. NMR chemical shift assignments are reported here for Ca<sup>2+</sup>-saturated CaM bound to the GluN2A C0 domain of NMDAR (BMRB no. 51821).</p></div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"17 1","pages":"89 - 93"},"PeriodicalIF":0.8000,"publicationDate":"2023-04-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s12104-023-10125-7.pdf","citationCount":"0","resultStr":"{\"title\":\"Chemical shift assignments of calmodulin bound to a cytosolic domain of GluN2A (residues 1004–1024) from the NMDA receptor\",\"authors\":\"Aritra Bej, James B. Ames\",\"doi\":\"10.1007/s12104-023-10125-7\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>N-methyl-D-aspartate receptors (NMDARs) consist of glycine-binding GluN1 and glutamate-binding GluN2 subunits that form tetrameric ion channels. NMDARs in the neuronal post-synaptic membrane are important for controlling neuroplasticity and synaptic transmission in the brain. Calmodulin (CaM) binds to the cytosolic C0 domains of both GluN1 (residues 841–865) and GluN2 (residues 1004–1024) that may play a role in the Ca<sup>2+</sup>-dependent desensitization of NMDAR channels. Mutations that disrupt Ca<sup>2+</sup>-dependent desensitization of NMDARs are linked to Alzheimer’s disease, depression, stroke, epilepsy, and schizophrenia. NMR chemical shift assignments are reported here for Ca<sup>2+</sup>-saturated CaM bound to the GluN2A C0 domain of NMDAR (BMRB no. 51821).</p></div>\",\"PeriodicalId\":492,\"journal\":{\"name\":\"Biomolecular NMR Assignments\",\"volume\":\"17 1\",\"pages\":\"89 - 93\"},\"PeriodicalIF\":0.8000,\"publicationDate\":\"2023-04-07\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://link.springer.com/content/pdf/10.1007/s12104-023-10125-7.pdf\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biomolecular NMR Assignments\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://link.springer.com/article/10.1007/s12104-023-10125-7\",\"RegionNum\":4,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q4\",\"JCRName\":\"BIOPHYSICS\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biomolecular NMR Assignments","FirstCategoryId":"99","ListUrlMain":"https://link.springer.com/article/10.1007/s12104-023-10125-7","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"BIOPHYSICS","Score":null,"Total":0}

引用次数: 0

摘要

n -甲基- d -天冬氨酸受体(NMDARs)由甘氨酸结合GluN1和谷氨酸结合GluN2亚基组成，形成四聚体离子通道。神经元突触后膜中的NMDARs对控制大脑神经可塑性和突触传递具有重要意义。钙调蛋白(CaM)结合GluN1(残基841-865)和GluN2(残基1004-1024)的细胞质C0结构域，可能在NMDAR通道的Ca2+依赖性脱敏中发挥作用。破坏NMDARs Ca2+依赖性脱敏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Ca2+饱和CaM与NMDAR (BMRB no. 1)的GluN2A C0结构域结合的NMR化学位移分配。51821)。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

Chemical shift assignments of calmodulin bound to a cytosolic domain of GluN2A (residues 1004–1024) from the NMDA receptor

查看原文本刊更多论文

Chemical shift assignments of calmodulin bound to a cytosolic domain of GluN2A (residues 1004–1024) from the NMDA receptor

N-methyl-D-aspartate receptors (NMDARs) consist of glycine-binding GluN1 and glutamate-binding GluN2 subunits that form tetrameric ion channels. NMDARs in the neuronal post-synaptic membrane are important for controlling neuroplasticity and synaptic transmission in the brain. Calmodulin (CaM) binds to the cytosolic C0 domains of both GluN1 (residues 841–865) and GluN2 (residues 1004–1024) that may play a role in the Ca²⁺-dependent desensitization of NMDAR channels. Mutations that disrupt Ca²⁺-dependent desensitization of NMDARs are linked to Alzheimer’s disease, depression, stroke, epilepsy, and schizophrenia. NMR chemical shift assignments are reported here for Ca²⁺-saturated CaM bound to the GluN2A C0 domain of NMDAR (BMRB no. 51821).

求助全文

通过发布文献求助，成功后即可免费获取论文全文。去求助

来源期刊

Biomolecular NMR Assignments 生物-光谱学

CiteScore

1.70

自引率

11.10%

发文量

审稿时长

6-12 weeks

期刊介绍： Biomolecular NMR Assignments provides a forum for publishing sequence-specific resonance assignments for proteins and nucleic acids as Assignment Notes. Chemical shifts for NMR-active nuclei in macromolecules contain detailed information on molecular conformation and properties. Publication of resonance assignments in Biomolecular NMR Assignments ensures that these data are deposited into a public database at BioMagResBank (BMRB; http://www.bmrb.wisc.edu/), where they are available to other researchers. Coverage includes proteins and nucleic acids; Assignment Notes are processed for rapid online publication and are published in biannual online editions in June and December.