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DOI | 10.1126/science.aaf9739 |
SIGNAL TRANSDUCTION Notch-Jagged complex structure implicates a catch bond in tuning ligand sensitivity | |
Luca, Vincent C.1,2,3; Kim, Byoung Choul4,5; Ge, Chenghao6; Kakuda, Shinako7; Wu, Di1,2,3; Roein-Peikar, Mehdi4,5,8; Haltiwanger, Robert S.7,11; Zhu, Cheng6,9; Ha, Taekjip4,5,8,10; Garcia, K. Christopher1,2,3 | |
2017-03-24 | |
发表期刊 | SCIENCE |
ISSN | 0036-8075 |
EISSN | 1095-9203 |
出版年 | 2017 |
卷号 | 355期号:6331页码:1320-+ |
文章类型 | Article |
语种 | 英语 |
国家 | USA |
英文摘要 | Notch receptor activation initiates cell fate decisions and is distinctive in its reliance on mechanical force and protein glycosylation. The 2.5-angstrom-resolution crystal structure of the extracellular interacting region of Notch1 complexed with an engineered, high-affinity variant of Jagged1 (Jag1) reveals a binding interface that extends similar to 120 angstroms along five consecutive domains of each protein. O-Linked fucose modifications on Notch1 epidermal growth factor-like (EGF) domains 8 and 12 engage the EGF3 and C2 domains of Jag1, respectively, and different Notch1 domains are favored in binding to Jag1 than those that bind to the Delta-like 4 ligand. Jag1 undergoes conformational changes upon Notch binding, exhibiting catch bond behavior that prolongs interactions in the range of forces required for Notch activation. This mechanism enables cellular forces to regulate binding, discriminate among Notch ligands, and potentiate Notch signaling. |
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:000397082900041 |
WOS关键词 | DELTA ; BINDING ; ACTIVATION ; DOMAIN ; ENDOCYTOSIS ; REGIONS ; FUCOSE ; SITES |
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/195691 |
专题 | 地球科学 资源环境科学 气候变化 |
作者单位 | 1.Stanford Univ, Sch Med, Dept Mol & Cellular Physiol, Stanford, CA 94305 USA; 2.Stanford Univ, Sch Med, Dept Biol Struct, Stanford, CA 94305 USA; 3.Howard Hughes Med Inst, Stanford, CA 94305 USA; 4.Howard Hughes Med Inst, Baltimore, MD 21205 USA; 5.Johns Hopkins Univ Sch Med, Dept Biomed Engn, Baltimore, MD 21205 USA; 6.Georgia Inst Technol, Dept Biomed Engn, Atlanta, GA 30332 USA; 7.SUNY Stony Brook, Dept Biochem & Cell Biol, Stony Brook, NY 11794 USA; 8.Johns Hopkins Univ Sch Med, Dept Biophys & Biophys Chem, Baltimore, MD 21205 USA; 9.Georgia Inst Technol, Woodruff Sch Mech Engn, Atlanta, GA 30332 USA; 10.Johns Hopkins Univ, Dept Biophys, Baltimore, MD 21218 USA; 11.Univ Georgia, Complex Carbohydrate Res Ctr, Athens, GA 30602 USA |
推荐引用方式 GB/T 7714 | Luca, Vincent C.,Kim, Byoung Choul,Ge, Chenghao,et al. SIGNAL TRANSDUCTION Notch-Jagged complex structure implicates a catch bond in tuning ligand sensitivity[J]. SCIENCE,2017,355(6331):1320-+. |
APA | Luca, Vincent C..,Kim, Byoung Choul.,Ge, Chenghao.,Kakuda, Shinako.,Wu, Di.,...&Garcia, K. Christopher.(2017).SIGNAL TRANSDUCTION Notch-Jagged complex structure implicates a catch bond in tuning ligand sensitivity.SCIENCE,355(6331),1320-+. |
MLA | Luca, Vincent C.,et al."SIGNAL TRANSDUCTION Notch-Jagged complex structure implicates a catch bond in tuning ligand sensitivity".SCIENCE 355.6331(2017):1320-+. |
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