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| - | [[Image:2bk0.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2bk0| PDB=2bk0 | SCENE= }} | | {{STRUCTURE_2bk0| PDB=2bk0 | SCENE= }} |
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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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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_16051263}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16051263 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_16051263}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Pathogenesis-related protein]] | | [[Category: Pathogenesis-related protein]] |
| | [[Category: Plant defense]] | | [[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 Tue Jul 29 04:19:43 2008'' |
Revision as of 01:19, 29 July 2008
Template:STRUCTURE 2bk0
CRYSTAL STRUCTURE OF THE MAJOR CELERY ALLERGEN API G 1
Template:ABSTRACT PUBMED 16051263
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 Tue Jul 29 04:19:43 2008
