2BK0

Crystal structure of the major celery allergen Api G 1

2BK0 の概要

• エントリーDOI: 10.2210/pdb2bk0/pdb
• 分子名称: MAJOR ALLERGEN API G 1 (1 entity in total)
• 機能のキーワード: major celery allergen api g 1, bet v 1-related protein, cross reactive epitopes, allergen, pathogenesis-related protein, plant defense
• 由来する生物種: APIUM GRAVEOLENS (CELERY)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 32669.17

構造登録者

Schirmer, T.,Hoffmann-Sommergruber, K.,Breiteneder, H.,Markovic-Housley, Z. (登録日: 2005-02-09, 公開日: 2005-06-13, 最終更新日: 2023-12-13)

主引用文献

Schirmer, T.,Hoffmann-Somergrube, K.,Susani, M.,Breiteneder, H.,Markovic-Housley, Z.
Crystal Structure of the Major Celery Allergen Api G 1: Molecular Analysis of Cross-Reactivity.
J.Mol.Biol., 351:1101-, 2005

PubMed Abstract: Many patients who have been sensitised to pollen, display allergic symptoms after ingestion of certain plant food such as fresh fruit, vegetables and nuts. The cause is the cross-reactivity between structurally very similar major plant allergens. In particular, allergy to celery is very frequently associated with birch and mugwort pollen sensitization, known as to the birch-mugwort-celery syndrome. The crystal structure of the major celery allergen Api g 1, a homologue of the major birch pollen allergen Bet v 1, has been determined to a resolution of 2.9 A. The structure of Api g 1 is very similar to that of Bet v 1 with major differences occurring in the segment comprised of residues 23-45, preceding the well conserved glycine-rich P-loop, as well as in loops beta3-beta4 and beta5-beta6. In particular, Api g 1 lacks E45, which has been shown to be a crucial residue for antibody recognition in the crystal complex of Bet v 1 with the Fab fragment of a murine monoclonal IgG (BV16) antibody. The absence of E45 and the structural differences in the preceding segment suggest that this region of the Api g 1 surface is probably not responsible for the observed cross-reactivity with Bet v 1. A detailed analysis of the molecular surface in combination with sequence alignment revealed three conserved surface patches which may account for cross-reactivity with Bet v 1. Several residues of Bet v 1 which have been shown by mutagenesis studies to be involved in IgE recognition belong to these conserved surface regions. The structure of Api g 1 and the related epitope analysis provides a molecular basis for a better understanding of allergen cross-reactivity and may lead to the development of hypoallergens which would allow a safer immunotherapy.

PubMed: 16051263
DOI: 10.1016/J.JMB.2005.06.054

実験手法

X-RAY DIFFRACTION (2.9 Å)