4BKD

Crystal Structure of an unusually linked dimeric variant of Bet v 1 (b)

4BKD の概要

• エントリーDOI: 10.2210/pdb4bkd/pdb
• 関連するPDBエントリー: 4BK6 4BK7 4BKC
• 分子名称: MAJOR POLLEN ALLERGEN BET V 1-A (2 entities in total)
• 機能のキーワード: allergen, dimerisation, polysulfide
• 由来する生物種: BETULA PENDULA (EUROPEAN WHITE BIRCH)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17529.82

構造登録者

Kofler, S.G.,Brandstetter, H. (登録日: 2013-04-23, 公開日: 2013-11-27, 最終更新日: 2024-11-13)

主引用文献

Kofler, S.,Ackaert, C.,Samonig, M.,Asam, C.,Briza, P.,Horejs-Hoeck, J.,Cabrele, C.,Ferreira, F.,Duschl, A.,Huber, C.,Brandstetter, H.
Stabilization of the dimeric birch pollen allergen Bet v 1 impacts its immunological properties.
J.Biol.Chem., 289:540-551, 2014

PubMed Abstract: Many allergens share several biophysical characteristics, including the capability to undergo oligomerization. The dimerization mechanism in Bet v 1 and its allergenic properties are so far poorly understood. Here, we report crystal structures of dimeric Bet v 1, revealing a noncanonical incorporation of cysteine at position 5 instead of genetically encoded tyrosine. Cysteine polysulfide bridging stabilized different dimeric assemblies, depending on the polysulfide linker length. These dimers represent quaternary arrangements that are frequently observed in related proteins, reflecting their prevalence in unmodified Bet v 1. These conclusions were corroborated by characteristic immunologic properties of monomeric and dimeric allergen variants. Hereby, residue 5 could be identified as an allergenic hot spot in Bet v 1. The presented results refine fundamental principles in protein chemistry and emphasize the importance of protein modifications in understanding the molecular basis of allergenicity.

PubMed: 24253036
DOI: 10.1074/jbc.M113.518795

実験手法

X-RAY DIFFRACTION (1.17 Å)