1llt

<table><tr><td colspan='2'>[[1llt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Betpn Betpn]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LLT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LLT FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1bv1|1bv1]], [[1btv|1btv]], [[1fsk|1fsk]], [[1qmr|1qmr]]</div></td></tr>

[[https://www.uniprot.org/uniprot/BEV1A_BETPN BEV1A_BETPN]] May be a general steroid carrier protein (By similarity).

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:12960334</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Betpn]]

[[Category: Gajhede, M]]

[[Category: Ipsen, H]]

[[Category: Larsen, J N]]

[[Category: Mirza, O]]

[[Category: Neerven, R J.Van]]

[[Category: Spangfort, M D]]

[[Category: Allergen]]

[[Category: Pathogenesis related protein]]