1e09

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[[Image:1e09.gif|left|200px]]
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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e09 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e09 OCA], [http://www.ebi.ac.uk/pdbsum/1e09 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1e09 RCSB]</span>
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'''SOLUTION STRUCTURE OF THE MAJOR CHERRY ALLERGEN PRU AV 1'''
'''SOLUTION STRUCTURE OF THE MAJOR CHERRY ALLERGEN PRU AV 1'''
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[[Category: Sticht, H.]]
[[Category: Sticht, H.]]
[[Category: Vieths, S.]]
[[Category: Vieths, S.]]
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[[Category: heteronuclear nmr]]
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[[Category: Heteronuclear nmr]]
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[[Category: major cherry allergen]]
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[[Category: Major cherry allergen]]
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[[Category: pathogenesis-related protein]]
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[[Category: Pathogenesis-related protein]]
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[[Category: structure]]
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[[Category: Structure]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:29:53 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:52:21 2008''
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Revision as of 11:29, 2 May 2008

Template:STRUCTURE 1e09

SOLUTION STRUCTURE OF THE MAJOR CHERRY ALLERGEN PRU AV 1


Overview

Birch pollinosis is often accompanied by hypersensitivity to fruit as a consequence of the cross-reaction of pollen allergen-specific IgE antibodies with homologous food proteins. To provide a basis for examining the cross-reactivity on a structural level, we used heteronuclear multidimensional NMR spectroscopy to determine the high-resolution three-dimensional structure of the major cherry allergen, Pru av 1, in solution. Based on a detailed comparison of the virtually identical structures of Pru av 1 and Bet v 1, the major birch pollen allergen, we propose an explanation for a significant aspect of the observed cross-reactivity pattern among the family of allergens under consideration. The large hydrophobic cavity expected to be important for the still unknown physiological function of Bet v 1 is conserved in Pru av 1. Structural homology to a domain of human MLN64 associated with cholesterol transport suggests phytosteroids as putative ligands for Pru av 1. NMR spectroscopy provides experimental evidence that Pru av 1 interacts with phytosteroids, and molecular modeling shows that the hydrophobic cavity is large enough to accommodate two such molecules.

About this Structure

1E09 is a Single protein structure of sequence from Prunus avium. Full crystallographic information is available from OCA.

Reference

Allergic cross-reactivity made visible: solution structure of the major cherry allergen Pru av 1., Neudecker P, Schweimer K, Nerkamp J, Scheurer S, Vieths S, Sticht H, Rosch P, J Biol Chem. 2001 Jun 22;276(25):22756-63. Epub 2001 Apr 3. PMID:11287426 Page seeded by OCA on Fri May 2 14:29:53 2008

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