2OO4
Structure of LNR-HD (Negative Regulatory Region) from human Notch 2
2OO4 の概要
| エントリーDOI | 10.2210/pdb2oo4/pdb |
| 分子名称 | Neurogenic locus notch homolog protein 2, CALCIUM ION, ZINC ION, ... (5 entities in total) |
| 機能のキーワード | alpha-beta-sandwich; sea domain; lnr; lin12 notch repeat; cysteine-rich; hd domain, cell cycle, signaling protein |
| 由来する生物種 | Homo sapiens (human) |
| 細胞内の位置 | Notch 2 extracellular truncation: Cell membrane ; Single-pass type I membrane protein . Notch 2 intracellular domain: Nucleus : Q04721 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 52972.31 |
| 構造登録者 | Gordon, W.R.,Vardar-Ulu, D.,Histen, G.,Sanchez-Irizarry, C.,Aster, J.C.,Blacklow, S.C. (登録日: 2007-01-25, 公開日: 2007-04-03, 最終更新日: 2024-11-20) |
| 主引用文献 | Gordon, W.R.,Vardar-Ulu, D.,Histen, G.,Sanchez-Irizarry, C.,Aster, J.C.,Blacklow, S.C. Structural basis for autoinhibition of Notch Nat.Struct.Mol.Biol., 14:295-300, 2007 Cited by PubMed Abstract: Notch receptors transmit signals between adjacent cells. Signaling is initiated when ligand binding induces metalloprotease cleavage of Notch within an extracellular negative regulatory region (NRR). We present here the X-ray structure of the human NOTCH2 NRR, which adopts an autoinhibited conformation. Extensive interdomain interactions within the NRR bury the metalloprotease site, showing that a substantial conformational movement is necessary to expose this site during activation by ligand. Leukemia-associated mutations in NOTCH1 probably release autoinhibition by destabilizing the conserved hydrophobic core of the NRR. PubMed: 17401372DOI: 10.1038/nsmb1227 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.003 Å) |
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