1llt
From Proteopedia
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| - | [[Image:1llt.gif|left|200px]] | + | [[Image:1llt.gif|left|200px]] |
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| - | '''BIRCH POLLEN ALLERGEN BET V 1 MUTANT E45S''' | + | {{Structure |
| + | |PDB= 1llt |SIZE=350|CAPTION= <scene name='initialview01'>1llt</scene>, resolution 3.10Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''BIRCH POLLEN ALLERGEN BET V 1 MUTANT E45S''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1LLT is a [ | + | 1LLT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Betula_pendula Betula pendula]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LLT OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12960334 12960334] |
[[Category: Betula pendula]] | [[Category: Betula pendula]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Spangfort, M D.]] | [[Category: Spangfort, M D.]] | ||
[[Category: allergen]] | [[Category: allergen]] | ||
| - | [[Category: pathogenesis related | + | [[Category: pathogenesis related protein]] |
| - | ''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 12:32:21 2008'' |
Revision as of 10:32, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
BIRCH POLLEN ALLERGEN BET V 1 MUTANT E45S
Overview
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.
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
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