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2LAG

Structure of the 44 kDa complex of interferon-alpha2 with the extracellular part of IFNAR2 obtained by 2D-double difference NOESY

2LAG の概要
エントリーDOI10.2210/pdb2lag/pdb
関連するPDBエントリー1kz1
NMR情報BMRB: 16677
分子名称Interferon alpha/beta receptor 2, Interferon alpha-2 (2 entities in total)
機能のキーワードinterferon, receptor, immune system
由来する生物種Homo sapiens (human)
詳細
細胞内の位置Secreted: P48551
Isoform 1: Membrane; Single-pass type I membrane protein. Isoform 2: Membrane; Single-pass type I membrane protein. Isoform 3: Secreted: P01563
タンパク質・核酸の鎖数2
化学式量合計43587.53
構造登録者
Nudelman, I.,Akabayov, S.R.,Scherf, T.,Anglister, J. (登録日: 2011-03-13, 公開日: 2011-08-17, 最終更新日: 2024-10-30)
主引用文献Nudelman, I.,Akabayov, S.R.,Scherf, T.,Anglister, J.
Observation of Intermolecular Interactions in Large Protein Complexes by 2D-Double Difference Nuclear Overhauser Enhancement Spectroscopy: Application to the 44 kDa Interferon-Receptor Complex.
J.Am.Chem.Soc., 133:14755-14764, 2011
Cited by
PubMed Abstract: NMR detection of intermolecular interactions between protons in large protein complexes is very challenging because it is difficult to distinguish between weak NOEs from intermolecular interactions and the much larger number of strong intramolecular NOEs. This challenging task is exacerbated by the decrease in signal-to-noise ratio in the often used isotope-edited and isotope-filtered experiments as a result of enhanced T(2) relaxation. Here, we calculate a double difference spectrum that shows exclusively intermolecular NOEs and manifests the good signal-to-noise ratio in 2D homonuclear NOESY spectra even for large proteins. The method is straightforward and results in a complete picture of all intermolecular interactions involving non exchangeable protons. Ninety-seven such (1)H-(1)H NOEs were assigned for the 44 KDa interferon-α2/IFNAR2 complex and used for docking these two proteins. The symmetry of the difference spectrum, its superb resolution, and unprecedented signal-to-noise ratio in this large protein/receptor complex suggest that this method is generally applicable to study large biopolymeric complexes.
PubMed: 21819146
DOI: 10.1021/ja205480v
主引用文献が同じPDBエントリー
実験手法
SOLUTION NMR
構造検証レポート
Validation report summary of 2lag
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2026-02-04に公開中

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