Solution structure of Der f 2, the major mite allergen for atopic diseases

被引:96
作者
Ichikawa, S
Hatanaka, H
Yuuki, T
Iwamoto, N
Kojima, S
Nishiyama, C
Ogura, K
Okumura, Y
Inagaki, F
机构
[1] Tokyo Metropolitan Inst Med Sci, Dept Mol Physiol, Bunkyo Ku, Tokyo 113, Japan
[2] Japan Womens Univ, Fac Sci, Dept Biol & Mat Sci, Bunkyo Ku, Tokyo 112, Japan
[3] Asahi Breweries Ltd, Biosci Res & Dev Lab, Ohta Ku, Tokyo 143, Japan
[4] RIKEN, Inst Phys & Chem Res, Tsukuba Life Sci Ctr, Lab Gene Technol & Safety, Ibaraki, Osaka 305, Japan
关键词
D O I
10.1074/jbc.273.1.356
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
House dust mites cause heavy atopic diseases such as asthma and dermatitis. Among allergens from Dermatophagoides farinae, Der f 2 shows the highest positive rate for atopic patients, but its biological function 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 spectroscopy. Der f 2 was found to be a single-domain protein of immunoglobulin fold, and its structure was the most similar to those of the two regulatory domains of transglutaminase, This fact, binding to the bacterial surface, and other small pieces of information hinted that Her f 2 is related to the innate antibacterial defense system in mites. The immunoglobulin E epitopes are also discussed on the basis of the tertiary structure.
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收藏
页码:356 / 360
页数:5
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