1llt

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[[Image:1llt.gif|left|200px]]
 
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{{Structure
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==BIRCH POLLEN ALLERGEN BET V 1 MUTANT E45S==
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|PDB= 1llt |SIZE=350|CAPTION= <scene name='initialview01'>1llt</scene>, resolution 3.10&Aring;
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<StructureSection load='1llt' size='340' side='right'caption='[[1llt]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<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>
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|ACTIVITY=
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</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>
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|GENE=
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<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>
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|DOMAIN=
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</table>
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|RELATEDENTRY=[[1bv1|1BV1]], [[1btv|1BTV]], [[1fsk|1FSK]], [[1qmr|1QMR]]
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== Function ==
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|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>
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[https://www.uniprot.org/uniprot/BEV1A_BETPN BEV1A_BETPN] May be a general steroid carrier protein (By similarity).
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}}
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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'''BIRCH POLLEN ALLERGEN BET V 1 MUTANT E45S'''
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ll/1llt_consurf.spt"</scriptWhenChecked>
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==Overview==
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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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.
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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==About this Structure==
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</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].
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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].
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<div style="clear:both"></div>
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__TOC__
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==Reference==
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</StructureSection>
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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]
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[[Category: Betula pendula]]
[[Category: Betula pendula]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Gajhede, M.]]
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[[Category: Gajhede M]]
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[[Category: Ipsen, H.]]
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[[Category: Ipsen H]]
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[[Category: Larsen, J N.]]
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[[Category: Larsen JN]]
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[[Category: Mirza, O.]]
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[[Category: Mirza O]]
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[[Category: Neerven, R J.Van.]]
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[[Category: Spangfort MD]]
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[[Category: Spangfort, M D.]]
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[[Category: Van Neerven RJ]]
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[[Category: allergen]]
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[[Category: pathogenesis related protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:04:22 2008''
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Current revision

BIRCH POLLEN ALLERGEN BET V 1 MUTANT E45S

PDB ID 1llt

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