4A87

Crystal Structure of Major Birch Pollen Allergen Bet v 1 a in complex with naringenin.

4A87 の概要

• エントリーDOI: 10.2210/pdb4a87/pdb
• 関連するPDBエントリー: 1B6F 1BTV 1BV1 1FSK 1LLT 1QMR 4A80 4A81 4A83 4A84 4A85 4A86 4A88
• 分子名称: MAJOR POLLEN ALLERGEN BET V 1-A, (4S)-2-METHYL-2,4-PENTANEDIOL, NARINGENIN, ... (6 entities in total)
• 機能のキーワード: allergen, pr-10 protein
• 由来する生物種: BETULA PENDULA (EUROPEAN WHITE BIRCH)
• 細胞内の位置: Cytoplasm: P15494
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18569.56

構造登録者

Kofler, S.,Brandstetter, H. (登録日: 2011-11-18, 公開日: 2012-05-30, 最終更新日: 2023-12-20)

主引用文献

Kofler, S.,Asam, C.,Eckhard, U.,Wallner, M.,Ferreira, F.,Brandstetter, H.
Crystallographically Mapped Ligand Binding Differs in High and Low Ige Binding Isoforms of Birch Pollen Allergen Bet V 1.
J.Mol.Biol., 422:109-, 2012

PubMed Abstract: The ability of pathogenesis-related proteins of family 10 to bind a broad spectrum of ligands is considered to play a key role for their physiological and pathological functions. In particular, Bet v 1, an archetypical allergen from birch pollen, is described as a highly promiscuous ligand acceptor. However, the detailed recognition mechanisms, including specificity factors discriminating binding properties of naturally occurring Bet v 1 variants, are poorly understood. Here, we report crystal structures of Bet v 1 variants in complex with an array of ligands at a resolution of up to 1.2 Å. Residue 30 within the hydrophobic pocket not only discriminates in high and low IgE binding Bet v 1 isoforms but also induces a drastic change in the binding mode of the model ligand deoxycholate. Ternary crystal structure complexes of Bet v 1 with several ligands together with the fluorogenic reporter 1-anilino-8-naphthalene sulfonate explain anomalous fluorescence binding curves obtained from 1-anilino-8-naphthalene sulfonate displacement assays. The structures reveal key interaction residues such as Tyr83 and rationalize both the binding specificity and promiscuity of the so-called hydrophobic pocket in Bet v 1. The intermolecular interactions of Bet v 1 reveal an unexpected complexity that will be indispensable to fully understand its roles within the physiological and allergenic context.

PubMed: 22634284
DOI: 10.1016/J.JMB.2012.05.016

実験手法

X-RAY DIFFRACTION (1.24 Å)