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5FM9

human Notch 1, EGF 4-7

5FM9 の概要
エントリーDOI10.2210/pdb5fm9/pdb
関連するPDBエントリー5FMA
分子名称NEUROGENIC LOCUS NOTCH HOMOLOG PROTEIN 1, CALCIUM ION (3 entities in total)
機能のキーワードtranscription, transmembrane, developmental, protein, notch signaling pathway, differentiation, phosphorylation, egf- like domain, regulation, receptor, activator, ank repeat, signalling, glycoprotein, extracellular, egf, notch, jagged, membrane
由来する生物種HOMO SAPIENS (HUMAN)
細胞内の位置Cell membrane ; Single-pass type I membrane protein . Notch 1 intracellular domain: Nucleus : P46531
タンパク質・核酸の鎖数1
化学式量合計16722.54
構造登録者
Weisshuhn, P.C.,Sheppard, D.,Taylor, P.,Whiteman, P.,Lea, S.M.,Handford, P.A.,Redfield, C. (登録日: 2015-11-02, 公開日: 2016-04-20, 最終更新日: 2024-01-10)
主引用文献Weisshuhn, P.C.,Sheppard, D.,Taylor, P.,Whiteman, P.,Lea, S.M.,Handford, P.A.,Redfield, C.
Non-Linear and Flexible Regions of the Human Notch1 Extracellular Domain Revealed by High-Resolution Structural Studies.
Structure, 24:555-, 2016
Cited by
PubMed Abstract: The Notch receptor is a key component of a core metazoan signaling pathway activated by Delta/Serrate/Lag-2 ligands expressed on an adjacent cell. This results in a short-range signal with profound effects on cell-fate determination, cell proliferation, and cell death. Key to understanding receptor function is structural knowledge of the large extracellular portion of Notch which contains multiple repeats of epidermal growth factor (EGF)-like domains. Here we investigate the EGF4-13 region of human Notch1 (hN1) using a multidisciplinary approach. Ca(2+)-binding measurements, X-ray crystallography, {(1)H}-(15)N heteronuclear nuclear Overhauser effects, and residual dipolar couplings support a non-linear organization for the EGF4-13 region with a rigid, bent conformation for EGF4-7 and a single flexible linkage between EGF9 and EGF10. These data allow us to construct an informed model for EGF10-13 which, in conjunction with comparative binding studies, demonstrates that EGF10 has an important role in determining Notch receptor sensitivity to Dll-4.
PubMed: 26996961
DOI: 10.1016/J.STR.2016.02.010
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.92 Å)
構造検証レポート
Validation report summary of 5fm9
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2024-10-30に公開中

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