1e09: Difference between revisions
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[[Image:1e09.gif|left|200px]] | [[Image:1e09.gif|left|200px]] | ||
'''SOLUTION STRUCTURE OF THE MAJOR CHERRY ALLERGEN PRU AV 1''' | {{Structure | ||
|PDB= 1e09 |SIZE=350|CAPTION= <scene name='initialview01'>1e09</scene> | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''SOLUTION STRUCTURE OF THE MAJOR CHERRY ALLERGEN PRU AV 1''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1E09 is a [ | 1E09 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Prunus_avium Prunus avium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E09 OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11287426 11287426] | ||
[[Category: Prunus avium]] | [[Category: Prunus avium]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: structure]] | [[Category: structure]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:47:23 2008'' | ||
Revision as of 08:47, 20 March 2008
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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
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