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DOI | 10.1126/science.aal3729 |
ION CHANNELS Cryo-EM structures of the triheteromeric NMDA receptor and its allosteric modulation | |
Lu, Wei1; Du, Juan1; Goehring, April1; Gouaux, Eric1,2 | |
2017-03-24 | |
发表期刊 | SCIENCE
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ISSN | 0036-8075 |
EISSN | 1095-9203 |
出版年 | 2017 |
卷号 | 355期号:6331 |
文章类型 | Article |
语种 | 英语 |
国家 | USA |
英文摘要 | N-methyl-D-aspartate receptors (NMDARs) are heterotetrameric ion channels assembled as diheteromeric or triheteromeric complexes. Here, we report structures of the triheteromeric GluN1/GluN2A/GluN2B receptor in the absence or presence of the GluN2B-specific allosteric modulator Ro 25-6981 (Ro), determined by cryogenic electron microscopy (cryo-EM). In the absence of Ro, the GluN2A and GluN2B amino-terminal domains (ATDs) adopt "closed" and "open" clefts, respectively. Upon binding Ro, the GluN2B ATD clamshell transitions from an open to a closed conformation. Consistent with a predominance of the GluN2A subunit in ion channel gating, the GluN2A subunit interacts more extensively with GluN1 subunits throughout the receptor, in comparison with the GluN2B subunit. Differences in the conformation of the pseudo-2-fold-related GluN1 subunits further reflect receptor asymmetry. The triheteromeric NMDAR structures provide the first view of the most common NMDA receptor assembly and show how incorporation of two different GluN2 subunits modifies receptor symmetry and subunit interactions, allowing each subunit to uniquely influence receptor structure and function, thus increasing receptor complexity. |
领域 | 地球科学 ; 气候变化 ; 资源环境 |
收录类别 | SCI-E |
WOS记录号 | WOS:000397082900029 |
WOS关键词 | AFFINITY ZINC INHIBITION ; D-ASPARTATE RECEPTOR ; X-RAY STRUCTURES ; SUBUNIT ARRANGEMENT ; CRYSTAL-STRUCTURE ; MOLECULAR-BASIS ; MECHANISM ; ACTIVATION ; DYNAMICS ; COMPLEXES |
WOS类目 | Multidisciplinary Sciences |
WOS研究方向 | Science & Technology - Other Topics |
URL | 查看原文 |
引用统计 | |
文献类型 | 期刊论文 |
条目标识符 | http://119.78.100.173/C666/handle/2XK7JSWQ/195679 |
专题 | 地球科学 资源环境科学 气候变化 |
作者单位 | 1.Oregon Hlth & Sci Univ, Vollum Inst, 3181 Southwest Sam Jackson Pk Rd, Portland, OR 97239 USA; 2.Oregon Hlth & Sci Univ, Howard Hughes Med Inst, 3181 Southwest Sam Jackson Pk Rd, Portland, OR USA |
推荐引用方式 GB/T 7714 | Lu, Wei,Du, Juan,Goehring, April,et al. ION CHANNELS Cryo-EM structures of the triheteromeric NMDA receptor and its allosteric modulation[J]. SCIENCE,2017,355(6331). |
APA | Lu, Wei,Du, Juan,Goehring, April,&Gouaux, Eric.(2017).ION CHANNELS Cryo-EM structures of the triheteromeric NMDA receptor and its allosteric modulation.SCIENCE,355(6331). |
MLA | Lu, Wei,et al."ION CHANNELS Cryo-EM structures of the triheteromeric NMDA receptor and its allosteric modulation".SCIENCE 355.6331(2017). |
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