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4zce

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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4zce FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zce OCA], [http://pdbe.org/4zce PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4zce RCSB], [http://www.ebi.ac.uk/pdbsum/4zce PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4zce FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zce OCA], [http://pdbe.org/4zce PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4zce RCSB], [http://www.ebi.ac.uk/pdbsum/4zce PDBsum]</span></td></tr>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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BACKGROUND: Der p 23 was recently identified in a European population as a major allergen and potentially a chitin binding protein. OBJECTIVE: This study sought to assess the importance of Der p 23 among other Dermatophagoides allergens in a North American population, and to determine the structure for functional characterization. METHODS: IgE binding to Der p 23, Der p 1, Der p 2, Der p 5, Der p 7, and Der p 8 was measured by ELISA. RNA-seq data from D. pteronyssinus were compared as estimates of allergen expression levels. The structure was analyzed by X-ray crystallography and NMR. RESULTS: Despite a high prevalence of Der p 23, (75% versus 87% and 79% for Der p 1 and Der p 2, respectively), the anti-Der p 23 IgE levels were relatively low. The patient response to the 6 allergens tested was variable (n=47), but on average anti-Der p 1 and anti-Der p 2 together accounted for 85% of the specific IgE. In terms of abundance, the RNA expression level of Der p 23 is the lowest of the major allergens, 30-fold less that Der p 1 and 7-fold less than Der p 2. The structure of Der p 23 is a small, globular protein stabilized by two disulfide bonds, which is structurally related to allergens such as Blo t 12 that contain carbohydrate binding domains that bind chitin. Functional assays failed to confirm chitin binding by Der p 23. CONCLUSIONS AND CLINICAL RELEVANCE: Der p 23 accounts for a small percentage of the IgE response to mite allergens, which is dominated by Der p 1 and Der p 2. The prevalence and amount of specific IgE to Der p 23 and Der p 2 are disproportionately high compared to abundance of other Dermatophagoides allergens. This article is protected by copyright. All rights reserved.
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Serological, genomic, and structural analyses of the major mite allergen Der p 23.,Mueller GA, Randall TA, Glesner J, Pedersen LC, Perera L, Edwards LL, DeRose EF, Chapman MD, London RE, Pomes A Clin Exp Allergy. 2015 Nov 25. doi: 10.1111/cea.12680. PMID:26602749<ref>PMID:26602749</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 4zce" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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</StructureSection>
</StructureSection>

Revision as of 07:21, 9 December 2015

Crystal Structure of the dust mite allergen Der p 23 from Dermatophagoides pteronyssinus

4zce, resolution 1.55Å

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