4DNS

Crystal structure of Bermuda grass isoallergen BG60 provides insight into the various cross-allergenicity of the pollen group 4 allergens

4DNS の概要

• エントリーDOI: 10.2210/pdb4dns/pdb
• 分子名称: FAD-linked oxidoreductase BG60, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, FLAVIN-ADENINE DINUCLEOTIDE, ... (5 entities in total)
• 機能のキーワード: fad binding domain, oxidoreductase
• 由来する生物種: Cynodon dactylon (Bermuda grass)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 112698.66

構造登録者

Huang, T.H.,Peng, H.J.,Su, S.N.,Liaw, S.H. (登録日: 2012-02-08, 公開日: 2012-12-05, 最終更新日: 2024-10-30)

主引用文献

Huang, T.H.,Peng, H.J.,Su, S.N.,Liaw, S.H.
Various cross-reactivity of the grass pollen group 4 allergens: crystallographic study of the Bermuda grass isoallergen Cyn d 4.
Acta Crystallogr.,Sect.D, 68:1303-1310, 2012

PubMed Abstract: The structure of Cyn d 4, the group 4 allergen from Bermuda grass, is reported at 2.15 Å resolution and is the first crystal structure of a naturally isolated pollen allergen. A conserved N-terminal segment that is only present in the large isoallergens forms extensive interactions with surrounding residues and hence greatly enhances the structural stability of the protein. Cyn d 4 contains an FAD cofactor that is covalently linked to His88 and Cys152. To date, all identified bicovalent flavoproteins are oxidases and their substrates are either sugars or secondary metabolites. A deep large hydrophobic substrate-binding cleft is present. Thus, Cyn d 4 may be an oxidase that is involved in the biosynthesis of a pollen-specific metabolite. Cyn d 4 shares ~70% sequence identity with the Pooideae group 4 allergens. Various cross-reactivities between grass pollen group 4 allergens have previously been demonstrated using sera from allergic patients. The protein surface displays an unusually large number of positively charged clusters, reflecting the high pI of ~10. 38 decapeptides that cover the solvent-accessible sequences did not show any significant IgE-binding activity using sera with high Cyn d 4 reactivity from four patients, suggesting that the IgE epitopes of Cyn d 4 are predominantly conformational in nature. Several group 4 structures were then modelled and their potential cross-reactive and species-specific IgE epitopes were proposed.

PubMed: 22993084
DOI: 10.1107/S0907444912027552

実験手法

X-RAY DIFFRACTION (2.15 Å)