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DOI	10.1073/pnas.2022933118
	The structure of a minimum amyloid fibril core formed by necroptosis-mediating RHIM of human RIPK3
	Wu X.; Ma Y.; Zhao K.; Zhang J.; Sun Y.; Li Y.; Dong X.; Hu H.; Liu J.; Wang J.; Zhang X.; Li B.; Wang H.; Li D.; Sun B.; Lu J.; Liu C.
发表日期	2021
ISSN	00278424
卷号	118 期号:14
英文摘要	Receptor-interacting protein kinases 3 (RIPK3), a central node in necroptosis, polymerizes in response to the upstream signals and then activates its downstream mediator to induce cell death. The active polymeric form of RIPK3 has been indicated as the form of amyloid fibrils assembled via its RIP homotypic interaction motif (RHIM). In this study, we combine cryogenic electron microscopy and solid-state NMR to determine the amyloid fibril structure of RIPK3 RHIM-containing C-terminal domain (CTD). The structure reveals a single protofilament composed of the RHIM domain. RHIM forms three β-strands (referred to as strands 1 through 3) folding into an S shape, a distinct fold from that in complex with RIPK1. The consensus tetrapeptide VQVG of RHIM forms strand 2, which zips up strands 1 and 3 via heterozipper-like interfaces. Notably, the RIPK3-CTD fibril, as a physiological fibril, exhibits distinctive assembly compared with pathological fibrils. It has an exceptionally small fibril core and twists in both handedness with the smallest pitch known so far. These traits may contribute to a favorable spatial arrangement of RIPK3 kinase domain for efficient phosphorylation. © 2021 National Academy of Sciences. All rights reserved.
英文关键词	Amyloid fibril; Cryo-EM; Necroptosis; SsNMR
语种	英语
scopus关键词	amyloid; receptor interacting protein kinase 3; receptor interacting protein serine threonine kinase; tetrapeptide; unclassified drug; valylglutamylvalylglycine tetrapeptide; Article; basic leucine zipper motif; carboxy terminal sequence; controlled study; cryoelectron microscopy; fibril; fibril core; human; human cell; necroptosis; nuclear magnetic resonance; nuclear shape; priority journal; protein folding; protein motif; protein phosphorylation; RIP homotypic interaction motif; structure analysis; thin filament
来源期刊	Proceedings of the National Academy of Sciences of the United States of America
文献类型	期刊论文
条目标识符	http://gcip.llas.ac.cn/handle/2XKMVOVA/179974
作者单位	School of Life Science and Technology, ShanghaiTech University, Shanghai, 201210, China; University of Chinese Academy of Sciences, Beijing, 100049, China; State Key Laboratory of Molecular Biology, CAS Center for Excellence in Molecular Cell Science, Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, Shanghai, 200031, China; Interdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai, 201210, China; Bio-X-Renji Hospital Research Center, Renji Hospital, School of Medicine, Shanghai Jiao Tong University, Shanghai, 200240, China; Bio-X Institutes, Key Laboratory for the Genetics of Developmental and Neuropsychiatric Disorders, Ministry of Education, Shanghai Jiao Tong University, Shanghai, 200030, China
推荐引用方式 GB/T 7714	Wu X.,Ma Y.,Zhao K.,et al. The structure of a minimum amyloid fibril core formed by necroptosis-mediating RHIM of human RIPK3[J],2021,118(14).
APA	Wu X..,Ma Y..,Zhao K..,Zhang J..,Sun Y..,...&Liu C..(2021).The structure of a minimum amyloid fibril core formed by necroptosis-mediating RHIM of human RIPK3.Proceedings of the National Academy of Sciences of the United States of America,118(14).
MLA	Wu X.,et al."The structure of a minimum amyloid fibril core formed by necroptosis-mediating RHIM of human RIPK3".Proceedings of the National Academy of Sciences of the United States of America 118.14(2021).