1llt: Difference between revisions

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[[Image:1llt.gif|left|200px]]


{{Structure
==BIRCH POLLEN ALLERGEN BET V 1 MUTANT E45S==
|PDB= 1llt |SIZE=350|CAPTION= <scene name='initialview01'>1llt</scene>, resolution 3.10&Aring;
<StructureSection load='1llt' size='340' side='right'caption='[[1llt]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<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>
|ACTIVITY=  
</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>
|GENE=  
<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>
|DOMAIN=
</table>
|RELATEDENTRY=[[1bv1|1BV1]], [[1btv|1BTV]], [[1fsk|1FSK]], [[1qmr|1QMR]]
== Function ==
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1llt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1llt OCA], [http://www.ebi.ac.uk/pdbsum/1llt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1llt RCSB]</span>
[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]]
'''BIRCH POLLEN ALLERGEN BET V 1 MUTANT E45S'''
Check<jmol>
 
  <jmolCheckbox>
 
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ll/1llt_consurf.spt"</scriptWhenChecked>
==Overview==
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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.
    <text>to colour the structure by Evolutionary Conservation</text>
 
  </jmolCheckbox>
==About this Structure==
</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].
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].  
<div style="clear:both"></div>
 
__TOC__
==Reference==
</StructureSection>
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: 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 protein]]
 
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Retrieved from "https://proteopedia.org/1llt"