4J4P

The complex of human IgE-Fc with two bound Fab fragments

4J4P の概要

• エントリーDOI: 10.2210/pdb4j4p/pdb
• 関連するPDBエントリー: 1LSO 2WQR 2Y7Q
• 分子名称: Ig epsilon chain C region, Immunoglobulin G Fab Fragment Heavy Chain, Immunoglobulin G Fab Fragment Light Chain, ... (5 entities in total)
• 機能のキーワード: ig like domain, immune system
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 177746.06

構造登録者

Drinkwater, N.,Sutton, B.J. (登録日: 2013-02-07, 公開日: 2014-03-12, 最終更新日: 2024-11-06)

主引用文献

Drinkwater, N.,Cossins, B.P.,Keeble, A.H.,Wright, M.,Cain, K.,Hailu, H.,Oxbrow, A.,Delgado, J.,Shuttleworth, L.K.,Kao, M.W.,McDonnell, J.M.,Beavil, A.J.,Henry, A.J.,Sutton, B.J.
Human immunoglobulin E flexes between acutely bent and extended conformations.
Nat.Struct.Mol.Biol., 21:397-404, 2014

PubMed Abstract: Crystallographic and solution studies have shown that IgE molecules are acutely bent in their Fc region. Crystal structures reveal the Cɛ2 domain pair folded back onto the Cɛ3-Cɛ4 domains, but is the molecule exclusively bent or can the Cɛ2 domains adopt extended conformations and even 'flip' from one side of the molecule to the other? We report the crystal structure of IgE-Fc captured in a fully extended, symmetrical conformation and show by molecular dynamics, calorimetry, stopped-flow kinetic, surface plasmon resonance (SPR) and Förster resonance energy transfer (FRET) analyses that the antibody can indeed adopt such extended conformations in solution. This diversity of conformational states available to IgE-Fc offers a new perspective on IgE function in allergen recognition, as part of the B-cell receptor and as a therapeutic target in allergic disease.

PubMed: 24632569
DOI: 10.1038/nsmb.2795

実験手法

X-RAY DIFFRACTION (2.91 Å)