2bk0
From Proteopedia
(New page: 200px<br /><applet load="2bk0" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bk0, resolution 2.90Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:2bk0.gif|left|200px]]<br /><applet load="2bk0" size=" | + | [[Image:2bk0.gif|left|200px]]<br /><applet load="2bk0" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2bk0, resolution 2.90Å" /> | caption="2bk0, resolution 2.90Å" /> | ||
'''CRYSTAL STRUCTURE OF THE MAJOR CELERY ALLERGEN API G 1'''<br /> | '''CRYSTAL STRUCTURE OF THE MAJOR CELERY ALLERGEN API G 1'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Many patients who have been sensitised to pollen, display allergic | + | 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== | ==About this Structure== | ||
| - | 2BK0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Apium_graveolens Apium graveolens]. Full crystallographic information is available from [http:// | + | 2BK0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Apium_graveolens Apium graveolens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BK0 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: plant defense]] | [[Category: plant defense]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:38:42 2008'' |
Revision as of 14:38, 21 February 2008
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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
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