SOLUTION STRUCTURE OF DER-F-2, THE MAJOR MITE ALLERGEN FOR ATOPIC DISEASES

Citation
S. Ichikawa et al., SOLUTION STRUCTURE OF DER-F-2, THE MAJOR MITE ALLERGEN FOR ATOPIC DISEASES, The Journal of biological chemistry, 273(1), 1998, pp. 356-360
Citations number
45
Categorie Soggetti
Biology
ISSN journal
00219258
Volume
273
Issue
1
Year of publication
1998
Pages
356 - 360
Database
ISI
SICI code
0021-9258(1998)273:1<356:SSODTM>2.0.ZU;2-I
Abstract
House dust mites cause heavy atopic diseases such as asthma and dermat itis. Among allergens from Dermatophagoides farinae, Der f 2 shows the highest positive rate for atopic patients, but its biological functio n in mites has been perfectly unknown, as well as the functions of its homologs in human and other animals. We have determined the tertiary structure of Der f 2 by multidimensional nuclear magnetic resonance sp ectroscopy. Der f 2 was found to be a single-domain protein of immunog lobulin fold, and its structure was the most similar to those of the t wo regulatory domains of transglutaminase, This fact, binding to the b acterial surface, and other small pieces of information hinted that He r f 2 is related to the innate antibacterial defense system in mites. The immunoglobulin E epitopes are also discussed on the basis of the t ertiary structure.