2j23

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[[Image:2j23.jpg|left|200px]]
 
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{{Structure
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==Cross-reactivity and crystal structure of Malassezia sympodialis Thioredoxin (Mala s 13), a member of a new pan-allergen family==
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|PDB= 2j23 |SIZE=350|CAPTION= <scene name='initialview01'>2j23</scene>, resolution 1.41&Aring;
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<StructureSection load='2j23' size='340' side='right'caption='[[2j23]], [[Resolution|resolution]] 1.41&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'>[[2j23]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Malassezia_sympodialis Malassezia sympodialis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J23 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J23 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]] 1.41&#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=2j23 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j23 OCA], [https://pdbe.org/2j23 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j23 RCSB], [https://www.ebi.ac.uk/pdbsum/2j23 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j23 ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2j23 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j23 OCA], [http://www.ebi.ac.uk/pdbsum/2j23 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2j23 RCSB]</span>
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[https://www.uniprot.org/uniprot/THIO_MALSM THIO_MALSM] Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions.<ref>PMID:17182577</ref> <ref>PMID:19032234</ref>
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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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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/j2/2j23_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=2j23 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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We have identified thioredoxins (Trx) of Malassezia sympodialis, a yeast involved in the pathogenesis of atopic eczema, and of Aspergillus fumigatus, a fungus involved in pulmonary complications, as novel IgE-binding proteins. We show that these Trx, including the human enzyme, represent cross-reactive structures recognized by serum IgE from individuals sensitized to M. sympodialis Trx. Moreover, all three proteins were able to elicit immediate-type allergic skin reactions in sensitized individuals, indicating a humoral immune response based on molecular mimicry. To analyze structural elements involved in these reactions, the three-dimensional structure of M. sympodialis Trx (Mala s 13) has been determined at 1.4-A resolution by x-ray diffraction analysis. The structure was solved by molecular replacement and refined to a crystallographic R factor of 14.0% and a free R factor of 16.8% and shows the typical Trx fold. Mala s 13 shares 45% sequence identity with human Trx and superposition of the solved Mala s 13 structure with those of human Trx reveals a high similarity with a root mean square deviation of 1.11 A for all Calpha atoms. In a detailed analysis of the molecular surface in combination with sequence alignment, we identified conserved solvent-exposed amino acids scattered over the surface in both structures which cluster to patches, thus forming putative conformational B cell epitopes potentially involved in IgE-mediated cross- and autoreactivity.
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'''CROSS-REACTIVITY AND CRYSTAL STRUCTURE OF MALASSEZIA SYMPODIALIS THIOREDOXIN (MALA S 13), A MEMBER OF A NEW PAN-ALLERGEN FAMILY'''
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Cross-reactivity and 1.4-A crystal structure of Malassezia sympodialis thioredoxin (Mala s 13), a member of a new pan-allergen family.,Limacher A, Glaser AG, Meier C, Schmid-Grendelmeier P, Zeller S, Scapozza L, Crameri R J Immunol. 2007 Jan 1;178(1):389-96. PMID:17182577<ref>PMID:17182577</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2j23" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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We have identified thioredoxins (Trx) of Malassezia sympodialis, a yeast involved in the pathogenesis of atopic eczema, and of Aspergillus fumigatus, a fungus involved in pulmonary complications, as novel IgE-binding proteins. We show that these Trx, including the human enzyme, represent cross-reactive structures recognized by serum IgE from individuals sensitized to M. sympodialis Trx. Moreover, all three proteins were able to elicit immediate-type allergic skin reactions in sensitized individuals, indicating a humoral immune response based on molecular mimicry. To analyze structural elements involved in these reactions, the three-dimensional structure of M. sympodialis Trx (Mala s 13) has been determined at 1.4-A resolution by x-ray diffraction analysis. The structure was solved by molecular replacement and refined to a crystallographic R factor of 14.0% and a free R factor of 16.8% and shows the typical Trx fold. Mala s 13 shares 45% sequence identity with human Trx and superposition of the solved Mala s 13 structure with those of human Trx reveals a high similarity with a root mean square deviation of 1.11 A for all Calpha atoms. In a detailed analysis of the molecular surface in combination with sequence alignment, we identified conserved solvent-exposed amino acids scattered over the surface in both structures which cluster to patches, thus forming putative conformational B cell epitopes potentially involved in IgE-mediated cross- and autoreactivity.
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*[[Thioredoxin 3D structures|Thioredoxin 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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2J23 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Malassezia_sympodialis Malassezia sympodialis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J23 OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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Cross-reactivity and 1.4-A crystal structure of Malassezia sympodialis thioredoxin (Mala s 13), a member of a new pan-allergen family., Limacher A, Glaser AG, Meier C, Schmid-Grendelmeier P, Zeller S, Scapozza L, Crameri R, J Immunol. 2007 Jan 1;178(1):389-96. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17182577 17182577]
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[[Category: Malassezia sympodialis]]
[[Category: Malassezia sympodialis]]
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[[Category: Single protein]]
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[[Category: Crameri R]]
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[[Category: Crameri, R.]]
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[[Category: Glaser AG]]
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[[Category: Glaser, A G.]]
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[[Category: Limacher A]]
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[[Category: Limacher, A.]]
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[[Category: Meier C]]
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[[Category: Meier, C.]]
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[[Category: Scapozza L]]
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[[Category: Scapozza, L.]]
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[[Category: allergen]]
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[[Category: autoreactivity]]
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[[Category: cross-reactivity]]
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[[Category: epitope]]
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[[Category: fungi]]
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[[Category: ige]]
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[[Category: immune protein]]
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[[Category: malassezia sympodiali]]
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[[Category: thioredoxin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:52:04 2008''
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Current revision

Cross-reactivity and crystal structure of Malassezia sympodialis Thioredoxin (Mala s 13), a member of a new pan-allergen family

PDB ID 2j23

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