Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedBirch 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
| ||||||||||||||||||
This page was last modified 07:57, 13 December 2017.