1e09
From Proteopedia
(New page: 200px<br /><applet load="1e09" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e09" /> '''SOLUTION STRUCTURE OF THE MAJOR CHERRY ALLER...) |
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| - | [[Image:1e09.gif|left|200px]]<br /><applet load="1e09" size=" | + | [[Image:1e09.gif|left|200px]]<br /><applet load="1e09" size="350" color="white" frame="true" align="right" spinBox="true" |
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'''SOLUTION STRUCTURE OF THE MAJOR CHERRY ALLERGEN PRU AV 1'''<br /> | '''SOLUTION STRUCTURE OF THE MAJOR CHERRY ALLERGEN PRU AV 1'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Birch pollinosis is often accompanied by hypersensitivity to fruit as a | + | 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== | ==About this Structure== | ||
| - | 1E09 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Prunus_avium Prunus avium]. Full crystallographic information is available from [http:// | + | 1E09 is a [http://en.wikipedia.org/wiki/Single_protein 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== | ||
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[[Category: structure]] | [[Category: structure]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:22:26 2008'' |
Revision as of 10:22, 21 February 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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