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| - | [[Image:1llt.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1llt.png|left|200px]] |
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| | {{STRUCTURE_1llt| PDB=1llt | SCENE= }} | | {{STRUCTURE_1llt| PDB=1llt | SCENE= }} |
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| - | '''BIRCH POLLEN ALLERGEN BET V 1 MUTANT E45S'''
| + | ===BIRCH POLLEN ALLERGEN BET V 1 MUTANT E45S=== |
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| - | ==Overview==
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| - | Specific allergy vaccination is an efficient treatment for allergic disease; however, the development of safer vaccines would enable a more general use of the treatment. Determination of molecular structures of allergens and allergen-Ab complexes facilitates epitope mapping and enables a rational approach to the engineering of allergen molecules with reduced IgE binding. In this study, we describe the identification and modification of a human IgE-binding epitope based on the crystal structure of Bet v 1 in complex with the BV16 Fab' fragment. The epitope occupies approximately 10% of the molecular surface area of Bet v 1 and is clearly conformational. A synthetic peptide representing a sequential motif in the epitope (11 of 16 residues) did not inhibit the binding of mAb BV16 to Bet v 1, illustrating limitations in the use of peptides for B cell epitope characterization. The single amino acid substitution, Glu(45)-Ser, was introduced in the epitope and completely abolished the binding of mAb BV16 to the Bet v 1 mutant within a concentration range 1000-fold higher than wild type. The mutant also showed up to 50% reduction in the binding of human polyclonal IgE, demonstrating that glutamic acid 45 is a critical amino acid also in a major human IgE-binding epitope. By solving the three-dimensional crystal structure of the Bet v 1 Glu(45)-Ser mutant, it was shown that the change in immunochemical activity is directly related to the Glu(45)-Ser substitution and not to long-range structural alterations or collapse of the Bet v 1 mutant tertiary structure.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_12960334}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 12960334 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_12960334}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Allergen]] | | [[Category: Allergen]] |
| | [[Category: Pathogenesis related protein]] | | [[Category: Pathogenesis related protein]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:02:47 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 21:23:43 2008'' |
Revision as of 18:23, 2 July 2008
Template:STRUCTURE 1llt
BIRCH POLLEN ALLERGEN BET V 1 MUTANT E45S
Template:ABSTRACT PUBMED 12960334
About this Structure
1LLT is a Single protein structure of sequence from Betula pendula. Full crystallographic information is available from OCA.
Reference
Dominating IgE-binding epitope of Bet v 1, the major allergen of birch pollen, characterized by X-ray crystallography and site-directed mutagenesis., Spangfort MD, Mirza O, Ipsen H, Van Neerven RJ, Gajhede M, Larsen JN, J Immunol. 2003 Sep 15;171(6):3084-90. PMID:12960334
Page seeded by OCA on Wed Jul 2 21:23:43 2008
