2bk0: Difference between revisions

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[[Image:2bk0.gif|left|200px]]<br /><applet load="2bk0" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:2bk0.gif|left|200px]]
caption="2bk0, resolution 2.90&Aring;" />
 
'''CRYSTAL STRUCTURE OF THE MAJOR CELERY ALLERGEN API G 1'''<br />
{{Structure
|PDB= 2bk0 |SIZE=350|CAPTION= <scene name='initialview01'>2bk0</scene>, resolution 2.90&Aring;
|SITE=
|LIGAND=
|ACTIVITY=
|GENE=
}}
 
'''CRYSTAL STRUCTURE OF THE MAJOR CELERY ALLERGEN API G 1'''
 


==Overview==
==Overview==
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==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://oca.weizmann.ac.il/oca-bin/ocashort?id=2BK0 OCA].  
2BK0 is a [[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==
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16051263 16051263]
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:[http://www.ncbi.nlm.nih.gov/pubmed/16051263 16051263]
[[Category: Apium graveolens]]
[[Category: Apium graveolens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: allergen]]
[[Category: allergen]]
[[Category: bet v 1-related protein]]
[[Category: bet v 1-related protein]]
[[Category: cross reactive epitopes]]
[[Category: cross reactive epitope]]
[[Category: major celery allergen api g 1]]
[[Category: major celery allergen api g 1]]
[[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 Thu Feb 21 16:38:42 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:02:58 2008''

Revision as of 17:03, 20 March 2008

File:2bk0.gif


PDB ID 2bk0

Drag the structure with the mouse to rotate
, resolution 2.90Å
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF THE MAJOR CELERY ALLERGEN API G 1


OverviewOverview

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 StructureAbout this Structure

2BK0 is a Single protein structure of sequence from Apium graveolens. Full crystallographic information is available from OCA.

ReferenceReference

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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