2j23
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
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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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[[Category: thioredoxin]] | [[Category: thioredoxin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:52:04 2008'' |
Revision as of 00:52, 31 March 2008
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| , resolution 1.41Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CROSS-REACTIVITY AND CRYSTAL STRUCTURE OF MALASSEZIA SYMPODIALIS THIOREDOXIN (MALA S 13), A MEMBER OF A NEW PAN-ALLERGEN FAMILY
Overview
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.
About this Structure
2J23 is a Single protein structure of sequence from Malassezia sympodialis. Full crystallographic information is available from OCA.
Reference
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
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