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5UK5

Complex of Notch1(EGF8-12) bound to Jagged1(N-EGF3)

5UK5 の概要
エントリーDOI10.2210/pdb5uk5/pdb
関連するPDBエントリー2VJ3 4CC0 4D0E 4XL1 4XLW
分子名称Neurogenic locus notch homolog protein 1, Protein jagged-1, alpha-D-xylopyranose-(1-3)-beta-D-glucopyranose, ... (9 entities in total)
機能のキーワードnotch, jagged, delta, glycoprotein, signaling protein
由来する生物種Rattus norvegicus (Rat)
詳細
タンパク質・核酸の鎖数2
化学式量合計59432.96
構造登録者
Garcia, K.C.,Luca, V.C. (登録日: 2017-01-19, 公開日: 2017-03-08, 最終更新日: 2023-10-04)
主引用文献Luca, V.C.,Kim, B.C.,Ge, C.,Kakuda, S.,Wu, D.,Roein-Peikar, M.,Haltiwanger, R.S.,Zhu, C.,Ha, T.,Garcia, K.C.
Notch-Jagged complex structure implicates a catch bond in tuning ligand sensitivity.
Science, 355:1320-1324, 2017
Cited by
PubMed Abstract: 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 ~120 angstroms along five consecutive domains of each protein. -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.
PubMed: 28254785
DOI: 10.1126/science.aaf9739
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.506 Å)
構造検証レポート
Validation report summary of 5uk5
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-12-31に公開中

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