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Atomic structures of FUS LC domain segments reveal bases for reversible amyloid fibril formation. FUS LC结构域片段的原子结构揭示了可逆淀粉样原纤维形成的基础。
IF 16.8 1区 生物学
Nature Structural &Molecular Biology Pub Date : 2018-04-01 DOI: 10.2210/PDB5XRR/PDB
F. Luo, X. Gui, Heng Zhou, Jinge Gu, Yichen Li, Xiangyu Liu, Minglei Zhao, Dan Li, Xueming Li, Cong Liu
{"title":"Atomic structures of FUS LC domain segments reveal bases for reversible amyloid fibril formation.","authors":"F. Luo, X. Gui, Heng Zhou, Jinge Gu, Yichen Li, Xiangyu Liu, Minglei Zhao, Dan Li, Xueming Li, Cong Liu","doi":"10.2210/PDB5XRR/PDB","DOIUrl":"https://doi.org/10.2210/PDB5XRR/PDB","url":null,"abstract":"Thermostable cross-β structures are characteristic of pathological amyloid fibrils, but these structures cannot explain the reversible nature of fibrils formed by RNA-binding proteins such as fused in sarcoma (FUS), involved in RNA granule assembly. Here, we find that two tandem (S/G)Y(S/G) motifs of the human FUS low-complexity domain (FUS LC) form reversible fibrils in a temperature- and phosphorylation-dependent manner. We named these motifs reversible amyloid cores, or RAC1 and RAC2, and determined their atomic structures in fibrillar forms, using microelectron and X-ray diffraction techniques. The RAC1 structure features an ordered-coil fibril spine rather than the extended β-strand typical of amyloids. Ser42, a phosphorylation site of FUS, is critical in the maintenance of the ordered-coil structure, which explains how phosphorylation controls fibril formation. The RAC2 structure shows a labile fibril spine with a wet interface. These structures illuminate the mechanism of reversible fibril formation and dynamic assembly of RNA granules.","PeriodicalId":18836,"journal":{"name":"Nature Structural &Molecular Biology","volume":"25 1","pages":"341-346"},"PeriodicalIF":16.8,"publicationDate":"2018-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"49353881","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: 22
Sub-ångström cryo-EM structure of a prion protofibril reveals a polar clasp 朊病毒原纤维的Sub-ångström冷冻电镜结构揭示了极性扣
IF 16.8 1区 生物学
Nature Structural &Molecular Biology Pub Date : 2018-01-17 DOI: 10.2210/PDB6AXZ/PDB
M. Gallagher-Jones, C. Glynn, D. Boyer, M. Martynowycz, Evelyn Hernandez, Jennifer Miao, Chih-Te Zee, I. Novikova, Lukasz Goldschmidt, Heather T Mcfarlane, G. Helguera, James E. Evans, M. Sawaya, D. Cascio, D. Eisenberg, T. Gonen, José A. Rodríguez
{"title":"Sub-ångström cryo-EM structure of a prion protofibril reveals a polar clasp","authors":"M. Gallagher-Jones, C. Glynn, D. Boyer, M. Martynowycz, Evelyn Hernandez, Jennifer Miao, Chih-Te Zee, I. Novikova, Lukasz Goldschmidt, Heather T Mcfarlane, G. Helguera, James E. Evans, M. Sawaya, D. Cascio, D. Eisenberg, T. Gonen, José A. Rodríguez","doi":"10.2210/PDB6AXZ/PDB","DOIUrl":"https://doi.org/10.2210/PDB6AXZ/PDB","url":null,"abstract":"The atomic structure of the infectious, protease-resistant, β-sheet-rich and fibrillar mammalian prion remains unknown. Through the cryo-EM method MicroED, we reveal the sub-angstrom-resolution structure of a protofibril formed by a wild-type segment from the β2–α2 loop of the bank vole prion protein. The structure of this protofibril reveals a stabilizing network of hydrogen bonds that link polar zippers within a sheet, producing motifs we have named ‘polar clasps’.","PeriodicalId":18836,"journal":{"name":"Nature Structural &Molecular Biology","volume":"25 1","pages":"131-134"},"PeriodicalIF":16.8,"publicationDate":"2018-01-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"45863239","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: 15
Guide bound structures of a divergent RNA-targeting A cleaving CRISPR-Cas13a enzyme 靶向分裂CRISPR-Cas13a酶的分化rna的引导结合结构
IF 16.8 1区 生物学
Nature Structural &Molecular Biology Pub Date : 2017-09-13 DOI: 10.2210/PDB5W1I/PDB
G. Knott, Alexandra East-Seletsky, Joshua C. Cofsky, J. Holton, E. Charles, J. Doudna
{"title":"Guide bound structures of a divergent RNA-targeting A cleaving CRISPR-Cas13a enzyme","authors":"G. Knott, Alexandra East-Seletsky, Joshua C. Cofsky, J. Holton, E. Charles, J. Doudna","doi":"10.2210/PDB5W1I/PDB","DOIUrl":"https://doi.org/10.2210/PDB5W1I/PDB","url":null,"abstract":"","PeriodicalId":18836,"journal":{"name":"Nature Structural &Molecular Biology","volume":"1 1","pages":""},"PeriodicalIF":16.8,"publicationDate":"2017-09-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"48346470","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
Selective Integrin Endocytosis is Driven by Alpha Chain:Ap2 Interactions 选择性整合素内吞作用由α链驱动:Ap2相互作用
IF 16.8 1区 生物学
Nature Structural &Molecular Biology Pub Date : 2016-01-18 DOI: 10.2210/PDB5FPI/PDB
N. D. Franceschi, Antti Arjonen, N. Elkhatib, K. Denessiouk, A. Wrobel, T. A. Wilson, J. Pouwels, Guillaume Montagnac, D. Owen, J. Ivaska
{"title":"Selective Integrin Endocytosis is Driven by Alpha Chain:Ap2 Interactions","authors":"N. D. Franceschi, Antti Arjonen, N. Elkhatib, K. Denessiouk, A. Wrobel, T. A. Wilson, J. Pouwels, Guillaume Montagnac, D. Owen, J. Ivaska","doi":"10.2210/PDB5FPI/PDB","DOIUrl":"https://doi.org/10.2210/PDB5FPI/PDB","url":null,"abstract":"We gratefully acknowledge the following funding sources: N.d.F. FinPharma Doctoral Program, Instrumentarium Foundation, Orion Research Foundation, Liv och Halsa foundation, Finsk-Norska Medicinska Stiftelsen and the Magnus Ehrnrooth Foundation; J.I. Academy of Finland CoE, European Research Council Consolidator Grant, the Sigrid Juselius Foundation, The Finnish Heart Foundation and Finnish Cancer Organizations. DJO, AGW and TW are funded by Wellcome Trust fellowship 090909 (DJO).","PeriodicalId":18836,"journal":{"name":"Nature Structural &Molecular Biology","volume":"23 1","pages":"172"},"PeriodicalIF":16.8,"publicationDate":"2016-01-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"68195440","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: 4
Cryo-Electron Microscopy of the Trpv2 Ion Channel Trpv2离子通道的低温电镜研究
IF 16.8 1区 生物学
Nature Structural &Molecular Biology Pub Date : 2016-01-01 DOI: 10.2210/PDB5AN8/PDB
L. Zubcevic, M. Herzik, B. C. Chung, G. Lander, Seok-Yong Lee
{"title":"Cryo-Electron Microscopy of the Trpv2 Ion Channel","authors":"L. Zubcevic, M. Herzik, B. C. Chung, G. Lander, Seok-Yong Lee","doi":"10.2210/PDB5AN8/PDB","DOIUrl":"https://doi.org/10.2210/PDB5AN8/PDB","url":null,"abstract":"","PeriodicalId":18836,"journal":{"name":"Nature Structural &Molecular Biology","volume":"23 1","pages":"180"},"PeriodicalIF":16.8,"publicationDate":"2016-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"68195129","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: 5
Crystal Structure of Broadly Neutralizing Antibody CH04, Isolated from Donor CH0219, in Complex with Scaffolded Trimeric HIV-1 Env V1V2 Domain from the Clade AE Strain A244 广泛中和抗体CH04与AE分支A244中支架三聚体HIV-1 Env V1V2结构域复合物的晶体结构
IF 16.8 1区 生物学
Nature Structural &Molecular Biology Pub Date : 2015-12-16 DOI: 10.2210/pdb5esz/pdb
J. Gorman, M. Yang, P. Kwong
{"title":"Crystal Structure of Broadly Neutralizing Antibody CH04, Isolated from Donor CH0219, in Complex with Scaffolded Trimeric HIV-1 Env V1V2 Domain from the Clade AE Strain A244","authors":"J. Gorman, M. Yang, P. Kwong","doi":"10.2210/pdb5esz/pdb","DOIUrl":"https://doi.org/10.2210/pdb5esz/pdb","url":null,"abstract":"","PeriodicalId":18836,"journal":{"name":"Nature Structural &Molecular Biology","volume":"1 1","pages":""},"PeriodicalIF":16.8,"publicationDate":"2015-12-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"68195423","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 of IFN receptor recognition by TYK2 TYK2识别IFN受体的结构基础
IF 16.8 1区 生物学
Nature Structural &Molecular Biology Pub Date : 2014-04-02 DOI: 10.2210/pdb4po6/pdb
H. Wallweber, C. Tam, Y. Franke, M. Starovasnik, P. Lupardus
{"title":"Structural basis of IFN receptor recognition by TYK2","authors":"H. Wallweber, C. Tam, Y. Franke, M. Starovasnik, P. Lupardus","doi":"10.2210/pdb4po6/pdb","DOIUrl":"https://doi.org/10.2210/pdb4po6/pdb","url":null,"abstract":"Tyrosine kinase 2 (TYK2) is a member of the Janus kinase (JAK) family of non-receptor tyrosine kinases, which are essential for proper signaling in immune responses and development. Here we present a 2.0 angstrom resolution crystal structure of a receptor-binding fragment of human TYK2 encompassing the FERM and SH2 domains in complex with a so-called “box2” containing intracellular peptide motif from the IFNα receptor (IFNAR1). The TYK2–IFNAR1 interface reveals an unexpected receptor-binding mode that mimics a SH2 domain–phosphopeptide interaction, with a glutamate replacing the canonical phosphotyrosine residue. This structure provides the first view to our knowledge of a JAK in complex with its cognate receptor and defines the molecular logic through which JAKs evolved to interact with divergent receptor sequences.","PeriodicalId":18836,"journal":{"name":"Nature Structural &Molecular Biology","volume":"21 1","pages":"443"},"PeriodicalIF":16.8,"publicationDate":"2014-04-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"68194115","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: 4
Structure of the retinoid X receptor alpha-liver X receptor beta (RXR alpha-LXR beta ) heterodimer on DNA. 类视黄醇X受体-肝X受体(RXR α - lxr β)异二聚体在DNA上的结构。
IF 16.8 1区 生物学
Nature Structural &Molecular Biology Pub Date : 2014-02-26 DOI: 10.2210/PDB4NQA/PDB
Xiaohua Lou, G. Toresson, Cindy Benod, J. Suh, Kevin J Philips, P. Webb, J. Gustafsson
{"title":"Structure of the retinoid X receptor alpha-liver X receptor beta (RXR alpha-LXR beta ) heterodimer on DNA.","authors":"Xiaohua Lou, G. Toresson, Cindy Benod, J. Suh, Kevin J Philips, P. Webb, J. Gustafsson","doi":"10.2210/PDB4NQA/PDB","DOIUrl":"https://doi.org/10.2210/PDB4NQA/PDB","url":null,"abstract":"","PeriodicalId":18836,"journal":{"name":"Nature Structural &Molecular Biology","volume":"21 1","pages":"277-281"},"PeriodicalIF":16.8,"publicationDate":"2014-02-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"68193982","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: 29
Research highlights 研究突出了
IF 16.8 1区 生物学
Nature Structural &Molecular Biology Pub Date : 2014-01-01 DOI: 10.3835/plantgenome2015.10.0001rh
Inês Chen, M. Hodges, S. Lall
{"title":"Research highlights","authors":"Inês Chen, M. Hodges, S. Lall","doi":"10.3835/plantgenome2015.10.0001rh","DOIUrl":"https://doi.org/10.3835/plantgenome2015.10.0001rh","url":null,"abstract":"volume 32 number 1 january 2014 nature biotechnology stem cell state10, we are likely witnessing the start of a reporting wave defining conditions for the generation of stable ICM-like human pluripotent stem cells. Given the importance of human pluripotency to the stem-cell field, confirmation of ICM-like pluripotency is essential. Like Higgs’ Boson to the field of particle physics, human ICM-like pluripotency was predicted from considerations of symmetry and conservation, and we are yet to unlock its potential.","PeriodicalId":18836,"journal":{"name":"Nature Structural &Molecular Biology","volume":"38 1","pages":"1245-1245"},"PeriodicalIF":16.8,"publicationDate":"2014-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"82721422","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
Nuclear membrane protein import 核膜蛋白输入
IF 16.8 1区 生物学
Nature Structural &Molecular Biology Pub Date : 2011-07-21 DOI: 10.1038/NSMB0711-747-PSI
A. Heinrichs
{"title":"Nuclear membrane protein import","authors":"A. Heinrichs","doi":"10.1038/NSMB0711-747-PSI","DOIUrl":"https://doi.org/10.1038/NSMB0711-747-PSI","url":null,"abstract":"","PeriodicalId":18836,"journal":{"name":"Nature Structural &Molecular Biology","volume":"100 1","pages":"747-747"},"PeriodicalIF":16.8,"publicationDate":"2011-07-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"57670245","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
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