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New page: left|200px<br /> <applet load="1llt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1llt, resolution 3.10Å" /> '''BIRCH POLLEN ALLERG...
 
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[[Image:1llt.gif|left|200px]]<br />
<applet load="1llt" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1llt, resolution 3.10&Aring;" />
'''BIRCH POLLEN ALLERGEN BET V 1 MUTANT E45S'''<br />


==Overview==
==BIRCH POLLEN ALLERGEN BET V 1 MUTANT E45S==
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.
<StructureSection load='1llt' size='340' side='right'caption='[[1llt]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1llt]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LLT FirstGlance]. <br>
1LLT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Betula_pendula Betula pendula]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LLT OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1&#8491;</td></tr>
 
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1llt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1llt OCA], [https://pdbe.org/1llt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1llt RCSB], [https://www.ebi.ac.uk/pdbsum/1llt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1llt ProSAT]</span></td></tr>
==Reference==
</table>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=12960334 12960334]
== Function ==
[https://www.uniprot.org/uniprot/BEV1A_BETPN BEV1A_BETPN] May be a general steroid carrier protein (By similarity).
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ll/1llt_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1llt ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Betula pendula]]
[[Category: Betula pendula]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Gajhede, M.]]
[[Category: Gajhede M]]
[[Category: Ipsen, H.]]
[[Category: Ipsen H]]
[[Category: Larsen, J.N.]]
[[Category: Larsen JN]]
[[Category: Mirza, O.]]
[[Category: Mirza O]]
[[Category: Neerven, R.J.Van.]]
[[Category: Spangfort MD]]
[[Category: Spangfort, M.D.]]
[[Category: Van Neerven RJ]]
[[Category: allergen]]
[[Category: pathogenesis related proteins]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 09:35:37 2007''

Latest revision as of 07:34, 14 February 2024

BIRCH POLLEN ALLERGEN BET V 1 MUTANT E45S

1llt, resolution 3.10Å

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