2bk0
From Proteopedia
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'''CRYSTAL STRUCTURE OF THE MAJOR CELERY ALLERGEN API G 1''' | '''CRYSTAL STRUCTURE OF THE MAJOR CELERY ALLERGEN API G 1''' | ||
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[[Category: Markovic-Housley, Z.]] | [[Category: Markovic-Housley, Z.]] | ||
[[Category: Schirmer, T.]] | [[Category: Schirmer, T.]] | ||
| - | [[Category: | + | [[Category: Allergen]] |
| - | [[Category: | + | [[Category: Bet v 1-related protein]] |
| - | [[Category: | + | [[Category: Cross reactive epitope]] |
| - | [[Category: | + | [[Category: Major celery allergen api g 1]] |
| - | [[Category: | + | [[Category: Pathogenesis-related protein]] |
| - | [[Category: | + | [[Category: Plant defense]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:23:39 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 17:23, 3 May 2008
CRYSTAL STRUCTURE OF THE MAJOR CELERY ALLERGEN API G 1
Overview
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.
About this Structure
2BK0 is a Single protein structure of sequence from Apium graveolens. Full crystallographic information is available from OCA.
Reference
Crystal structure of the major celery allergen Api g 1: molecular analysis of cross-reactivity., Schirmer T, Hoffimann-Sommergrube K, Susani M, Breiteneder H, Markovic-Housley Z, J Mol Biol. 2005 Sep 2;351(5):1101-9. PMID:16051263 Page seeded by OCA on Sat May 3 20:23:39 2008
