2VXQ

Crystal structure of the major grass pollen allergen Phl p 2 in complex with its specific IgE-Fab

2VXQ の概要

• エントリーDOI: 10.2210/pdb2vxq/pdb
• 関連するPDBエントリー: 1BMW 1WHO 1WHP
• 分子名称: POLLEN ALLERGEN PHL P 2, FAB, ... (4 entities in total)
• 機能のキーワード: receptor, secreted, rphl p 2, allergen, allergen-ige fab complex, recombinant grass pollen allergen
• 由来する生物種: PHLEUM PRATENSE (COMMON TIMOTHY); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 57249.81

構造登録者

Padavattan, S.,Flicker, S.,Schirmer, T.,Madritsch, C.,Randow, S.,Reese, G.,Vieths, S.,Lupinek, C.,Ebner, C.,Valenta, R.,Markovic-Housley, Z. (登録日: 2008-07-08, 公開日: 2009-02-17, 最終更新日: 2024-10-16)

主引用文献

Padavattan, S.,Flicker, S.,Schirmer, T.,Madritsch, C.,Randow, S.,Reese, G.,Vieths, S.,Lupinek, C.,Ebner, C.,Valenta, R.,Markovic-Housley, Z.
High-Affinity Ige Recognition of a Conformational Epitope of the Major Respiratory Allergen Phl P 2 as Revealed by X-Ray Crystallography.
J.Immunol., 182:2141-, 2009

PubMed Abstract: We report the three-dimensional structure of the complex between the major respiratory grass pollen allergen Phl p 2 and its specific human IgE-derived Fab. The Phl p 2-specific human IgE Fab has been isolated from a combinatorial library constructed from lymphocytes of a pollen allergic patient. When the variable domains of the IgE Fab were grafted onto human IgG1, the resulting Ab (huMab2) inhibited strongly the binding of allergic patients' IgE to Phl p 2 as well as allergen-induced basophil degranulation. Analysis of the binding of the allergen to the Ab by surface plasmon resonance yielded a very low dissociation constant (K(D) = 1.1 x 10(-10) M), which is similar to that between IgE and Fcepsilon;RI. The structure of the Phl p 2/IgE Fab complex was determined by x-ray crystallography to 1.9 A resolution revealing a conformational epitope (876 A(2)) comprised of the planar surface of the four-stranded anti-parallel beta-sheet of Phl p 2. The IgE-defined dominant epitope is discontinuous and formed by 21 residues located mostly within the beta strands. Of the 21 residues, 9 interact directly with 5 of the 6 CDRs (L1, L3, H1, H2, H3) of the IgE Fab predominantly by hydrogen bonding and van der Waals interactions. Our results indicate that IgE Abs recognize conformational epitopes with high affinity and provide a structural basis for the highly efficient effector cell activation by allergen/IgE immune complexes.

PubMed: 19201867
DOI: 10.4049/JIMMUNOL.0803018

実験手法

X-RAY DIFFRACTION (1.9 Å)