1AHK
DER F 2, THE MAJOR MITE ALLERGEN FROM DERMATOPHAGOIDES FARINAE, NMR, MINIMIZED AVERAGE STRUCTURE
Summary for 1AHK
| Entry DOI | 10.2210/pdb1ahk/pdb |
| Descriptor | DER F 2 (1 entity in total) |
| Functional Keywords | allergen, immunoglobulin fold |
| Biological source | Dermatophagoides farinae (American house dust mite) |
| Total number of polymer chains | 1 |
| Total formula weight | 14064.19 |
| Authors | Ichikawa, S.,Hatanaka, H.,Yuuki, T.,Iwamoto, N.,Ogura, K.,Okumura, Y.,Inagaki, F. (deposition date: 1997-04-07, release date: 1998-04-08, Last modification date: 2024-10-30) |
| Primary citation | Ichikawa, S.,Hatanaka, H.,Yuuki, T.,Iwamoto, N.,Kojima, S.,Nishiyama, C.,Ogura, K.,Okumura, Y.,Inagaki, F. Solution structure of Der f 2, the major mite allergen for atopic diseases. J.Biol.Chem., 273:356-360, 1998 Cited by PubMed Abstract: 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 Der 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. PubMed: 9417088DOI: 10.1074/jbc.273.1.356 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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