Nature Structural & Molecular Biology最新文献_第2页

Publisher Correction: Structure and activation of the RING E3 ubiquitin ligase TRIM72 on the membrane 出版商更正：RING E3 泛素连接酶 TRIM72 在膜上的结构和活化。

IF 12.5 1区生物学

Nature Structural & Molecular Biology Pub Date : 2024-10-28 DOI: 10.1038/s41594-024-01429-w

Si Hoon Park, Juhyun Han, Byung-Cheon Jeong, Ju Han Song, Se Hwan Jang, Hyeongseop Jeong, Bong Heon Kim, Young-Gyu Ko, Zee-Yong Park, Kyung Eun Lee, Jaekyung Hyun, Hyun Kyu Song

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Author Correction: Structural basis for antibody-mediated NMDA receptor clustering and endocytosis in autoimmune encephalitis 作者更正：自身免疫性脑炎中抗体介导的 NMDA 受体聚集和内吞的结构基础

IF 12.5 1区生物学

Nature Structural & Molecular Biology Pub Date : 2024-10-25 DOI: 10.1038/s41594-024-01410-7

Han Wang, Chun Xie, Bo Deng, Jinjun Ding, Na Li, Zengwei Kou, Mengmeng Jin, Jie He, Qinrui Wang, Han Wen, Jinbao Zhang, Qinming Zhou, Sheng Chen, Xiangjun Chen, Ti-Fei Yuan, Shujia Zhu

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Clamping Pol ε to the leading strand 将 Pol ε 夹在前导链上

IF 12.5 1区生物学

Nature Structural & Molecular Biology Pub Date : 2024-10-22 DOI: 10.1038/s41594-024-01416-1

Noopur Singh, Erik Johansson

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Cohesin closes the door on coexpression 聚合素关闭了共表达之门

IF 12.5 1区生物学

Nature Structural & Molecular Biology Pub Date : 2024-10-15 DOI: 10.1038/s41594-024-01404-5

George Andrew S. Inglis

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Insights into reproduction-regulating NOD-like receptors 对生殖调节 NOD 样受体的深入了解

IF 12.5 1区生物学

Nature Structural & Molecular Biology Pub Date : 2024-10-08 DOI: 10.1038/s41594-024-01383-7

Inga V. Hochheiser, Matthias Geyer

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Cryo-EM structure of the human subcortical maternal complex and the associated discovery of infertility-associated variants 人类皮层下母体复合体的低温电子显微镜结构及不孕症相关变体的发现

IF 12.5 1区生物学

Nature Structural & Molecular Biology Pub Date : 2024-10-08 DOI: 10.1038/s41594-024-01396-2

Pengliang Chi, Guojin Ou, Sibei Liu, Qianhong Ma, Yuechao Lu, Jinhong Li, Jialu Li, Qianqian Qi, Zhuo Han, Zihan Zhang, Qingting Liu, Li Guo, Jing Chen, Xiang Wang, Wei Huang, Lei Li, Dong Deng

{"title":"Cryo-EM structure of the human subcortical maternal complex and the associated discovery of infertility-associated variants","authors":"Pengliang Chi, Guojin Ou, Sibei Liu, Qianhong Ma, Yuechao Lu, Jinhong Li, Jialu Li, Qianqian Qi, Zhuo Han, Zihan Zhang, Qingting Liu, Li Guo, Jing Chen, Xiang Wang, Wei Huang, Lei Li, Dong Deng","doi":"10.1038/s41594-024-01396-2","DOIUrl":"10.1038/s41594-024-01396-2","url":null,"abstract":"The functionally conserved subcortical maternal complex (SCMC) is essential for early embryonic development in mammals. Reproductive disorders caused by pathogenic variants in NLRP5, TLE6 and OOEP, three core components of the SCMC, have attracted much attention over the past several years. Evaluating the pathogenicity of a missense variant in the SCMC is limited by the lack of information on its structure, although we recently solved the structure of the mouse SCMC and proposed that reproductive disorders caused by pathogenic variants are related to the destabilization of the SCMC core complex. Here we report the cryogenic electron microscopy structure of the human SCMC and uncover that the pyrin domain of NLRP5 is essential for the stability of SCMC. By combining prediction of SCMC stability and in vitro reconstitution, we provide a method for identifying deleterious variants, and we successfully identify a new pathogenic variant of TLE6 (p.A396T). Thus, on the basis of the structure of the human SCMC, we offer a strategy for the diagnosis of reproductive disorders and the discovery of new infertility-associated variants. On the basis of the assembly mechanism and structures of the human subcortical maternal complex, the authors provide a strategy for the diagnosis of reproductive disorders and the discovery of new infertility-associated SCMC variants.","PeriodicalId":49141,"journal":{"name":"Nature Structural & Molecular Biology","volume":"31 11","pages":"1798-1807"},"PeriodicalIF":12.5,"publicationDate":"2024-10-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142384213","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Publisher Correction: Structural basis of LRPPRC–SLIRP-dependent translation by the mitoribosome 出版商更正：mitoribosome依赖LRPPRC-SLIRP翻译的结构基础。

IF 12.5 1区生物学

Nature Structural & Molecular Biology Pub Date : 2024-09-19 DOI: 10.1038/s41594-024-01402-7

Vivek Singh, J. Conor Moran, Yuzuru Itoh, Iliana C. Soto, Flavia Fontanesi, Mary Couvillion, Martijn A. Huynen, L. Stirling Churchman, Antoni Barrientos, Alexey Amunts

引用次数: 0

Author Correction: Unwinding of a eukaryotic origin of replication visualized by cryo-EM 作者更正：用低温电子显微镜观察真核生物复制起源的开卷。

IF 12.5 1区生物学

Nature Structural & Molecular Biology Pub Date : 2024-09-09 DOI: 10.1038/s41594-024-01398-0

Sarah S. Henrikus, Marta H. Gross, Oliver Willhoft, Thomas Pühringer, Jacob S. Lewis, Allison W. McClure, Julia F. Greiwe, Giacomo Palm, Andrea Nans, John F. X. Diffley, Alessandro Costa

引用次数: 0

Structural and functional mechanisms of anti-NMDAR autoimmune encephalitis 抗 NMDAR 自身免疫性脑炎的结构和功能机制

IF 12.5 1区生物学

Nature Structural & Molecular Biology Pub Date : 2024-09-03 DOI: 10.1038/s41594-024-01386-4

Kevin Michalski, Taha Abdulla, Sam Kleeman, Lars Schmidl, Ricardo Gómez, Noriko Simorowski, Francesca Vallese, Harald Prüss, Manfred Heckmann, Christian Geis, Hiro Furukawa

{"title":"Structural and functional mechanisms of anti-NMDAR autoimmune encephalitis","authors":"Kevin Michalski, Taha Abdulla, Sam Kleeman, Lars Schmidl, Ricardo Gómez, Noriko Simorowski, Francesca Vallese, Harald Prüss, Manfred Heckmann, Christian Geis, Hiro Furukawa","doi":"10.1038/s41594-024-01386-4","DOIUrl":"10.1038/s41594-024-01386-4","url":null,"abstract":"Autoantibodies against neuronal membrane proteins can manifest in autoimmune encephalitis, inducing seizures, cognitive dysfunction and psychosis. Anti-N-methyl-d-aspartate receptor (NMDAR) encephalitis is the most dominant autoimmune encephalitis; however, insights into how autoantibodies recognize and alter receptor functions remain limited. Here we determined structures of human and rat NMDARs bound to three distinct patient-derived antibodies using single-particle electron cryo-microscopy. These antibodies bind different regions within the amino-terminal domain of the GluN1 subunit. Through electrophysiology, we show that all three autoantibodies acutely and directly reduced NMDAR channel functions in primary neurons. Antibodies show different stoichiometry of binding and antibody–receptor complex formation, which in one antibody, 003-102, also results in reduced synaptic localization of NMDARs. These studies demonstrate mechanisms of diverse epitope recognition and direct channel regulation of anti-NMDAR autoantibodies underlying autoimmune encephalitis. Anti-NMDA receptor encephalitis is the most common autoimmune encephalitis. Michalski et al. reveal epitope diversity, conformational changes and functional impacts of the autoantibodies using cryo-EM and electrophysiology.","PeriodicalId":49141,"journal":{"name":"Nature Structural & Molecular Biology","volume":"31 12","pages":"1975-1986"},"PeriodicalIF":12.5,"publicationDate":"2024-09-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142123517","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Structural basis for antibody-mediated NMDA receptor clustering and endocytosis in autoimmune encephalitis 自身免疫性脑炎中抗体介导的 NMDA 受体聚集和内吞的结构基础

IF 12.5 1区生物学

Nature Structural & Molecular Biology Pub Date : 2024-09-03 DOI: 10.1038/s41594-024-01387-3

Han Wang, Chun Xie, Bo Deng, Jinjun Ding, Na Li, Zengwei Kou, Mengmeng Jin, Jie He, Qinrui Wang, Han Wen, Jinbao Zhang, Qinming Zhou, Sheng Chen, Xiangjun Chen, Ti-Fei Yuan, Shujia Zhu

{"title":"Structural basis for antibody-mediated NMDA receptor clustering and endocytosis in autoimmune encephalitis","authors":"Han Wang, Chun Xie, Bo Deng, Jinjun Ding, Na Li, Zengwei Kou, Mengmeng Jin, Jie He, Qinrui Wang, Han Wen, Jinbao Zhang, Qinming Zhou, Sheng Chen, Xiangjun Chen, Ti-Fei Yuan, Shujia Zhu","doi":"10.1038/s41594-024-01387-3","DOIUrl":"10.1038/s41594-024-01387-3","url":null,"abstract":"Antibodies against N-methyl-d-aspartate receptors (NMDARs) are most frequently detected in persons with autoimmune encephalitis (AE) and used as diagnostic biomarkers. Elucidating the structural basis of monoclonal antibody (mAb) binding to NMDARs would facilitate the development of targeted therapy for AE. Here, we reconstructed nanodiscs containing green fluorescent protein-fused NMDARs to label and sort individual immune B cells from persons with AE and further cloned and identified mAbs against NMDARs. This allowed cryo-electron microscopy analysis of NMDAR–Fab complexes, revealing that autoantibodies bind to the R1 lobe of the N-terminal domain of the GluN1 subunit. Small-angle X-ray scattering studies demonstrated NMDAR–mAb stoichiometry of 2:1 or 1:2, structurally suitable for mAb-induced clustering and endocytosis of NMDARs. Importantly, these mAbs reduced the surface NMDARs and NMDAR-mediated currents, without tonically affecting NMDAR channel gating. These structural and functional findings imply that the design of neutralizing antibody binding to the R1 lobe of NMDARs represents a potential therapy for AE treatment. The authors cloned anti-NMDAR (N-methyl-d-aspartate receptor) monoclonal antibodies from the immune B cells of persons with autoimmune encephalitis and revealed their precise binding epitopes on NMDARs and the pathological mechanism underlying the downregulation of synaptic function.","PeriodicalId":49141,"journal":{"name":"Nature Structural & Molecular Biology","volume":"31 12","pages":"1987-1996"},"PeriodicalIF":12.5,"publicationDate":"2024-09-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.nature.com/articles/s41594-024-01387-3.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142123520","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0