Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Suzuki M, Tanaka Y, Korematsu S, Mikami B, Minato N. Crystal structure and some properties of a major house dust mite allergen, Derf 2. Biochem Biophys Res Commun. 2006 Jan 13;339(2):679-86. Epub 2005 Nov 21. PMID:16313885 doi:10.1016/j.bbrc.2005.11.065
