2f08
From Proteopedia
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| - | [[Image:2f08.gif|left|200px]]<br /><applet load="2f08" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2f08, resolution 2.20Å" /> | ||
| - | '''Crystal structure of a major house dust mite allergen, Derf 2'''<br /> | ||
| - | == | + | ==Crystal structure of a major house dust mite allergen, Derf 2== |
| + | <StructureSection load='2f08' size='340' side='right'caption='[[2f08]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2f08]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/American_house_dust_mite American house dust mite]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F08 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2F08 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=P4C:O-ACETALDEHYDYL-HEXAETHYLENE+GLYCOL'>P4C</scene></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=2f08 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f08 OCA], [https://pdbe.org/2f08 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2f08 RCSB], [https://www.ebi.ac.uk/pdbsum/2f08 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2f08 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == 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/f0/2f08_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=2f08 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
Pyroglyphid house dust mites are a major source of allergens in house dust. Mite allergens sensitize and induce asthma, rhinitis, and eczema in a large portion of patients with allergic diseases. Here, the crystal structure of a major mite allergen, Derf 2, derived from Dermatophagoides farinae was solved by single isomorphous replacement method with anomalous scattering (SIRAS) at 2.1A resolution. The present study also demonstrated that the conformation of the allergen was critical in the determination of Th1/Th2 shift based on physicochemical and immunological analyses. This indicates that rigidly folded and singly dispersed structure is essentially required for the generation of Th2 type cells by the allergen, while conformational variant protein leads to Th1 skewing, irrespective of the same amino acid sequence. This structure/function relationship may allow us to develop a novel strategy for hyposensitization therapy in patients with allergic diseases triggered by house dust mite allergens. | Pyroglyphid house dust mites are a major source of allergens in house dust. Mite allergens sensitize and induce asthma, rhinitis, and eczema in a large portion of patients with allergic diseases. Here, the crystal structure of a major mite allergen, Derf 2, derived from Dermatophagoides farinae was solved by single isomorphous replacement method with anomalous scattering (SIRAS) at 2.1A resolution. The present study also demonstrated that the conformation of the allergen was critical in the determination of Th1/Th2 shift based on physicochemical and immunological analyses. This indicates that rigidly folded and singly dispersed structure is essentially required for the generation of Th2 type cells by the allergen, while conformational variant protein leads to Th1 skewing, irrespective of the same amino acid sequence. This structure/function relationship may allow us to develop a novel strategy for hyposensitization therapy in patients with allergic diseases triggered by house dust mite allergens. | ||
| - | + | Crystal structure and some properties of a major house dust mite allergen, Derf 2.,Suzuki M, Tanaka Y, Korematsu S, Mikami B, Minato N Biochem Biophys Res Commun. 2006 Jan 13;339(2):679-86. Epub 2005 Nov 21. PMID:16313885<ref>PMID:16313885</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: | + | <div class="pdbe-citations 2f08" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: Korematsu, S | + | <references/> |
| - | [[Category: Mikami, B | + | __TOC__ |
| - | [[Category: Minato, N | + | </StructureSection> |
| - | [[Category: Suzuki, M | + | [[Category: American house dust mite]] |
| - | [[Category: Tanaka, Y | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Korematsu, S]] |
| - | [[Category: | + | [[Category: Mikami, B]] |
| - | + | [[Category: Minato, N]] | |
| - | + | [[Category: Suzuki, M]] | |
| + | [[Category: Tanaka, Y]] | ||
| + | [[Category: Immune system]] | ||
| + | [[Category: Immunoglobulin fold]] | ||
Current revision
Crystal structure of a major house dust mite allergen, Derf 2
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