1WRF
Refined solution structure of Der f 2, The Major Mite Allergen from Dermatophagoides farinae
Summary for 1WRF
| Entry DOI | 10.2210/pdb1wrf/pdb |
| Related | 1AHK 1AHM |
| Descriptor | Mite group 2 allergen Der f 2 (1 entity in total) |
| Functional Keywords | allergen, immunoglobulin fold |
| Biological source | Dermatophagoides farinae (American house dust mite) |
| Cellular location | Secreted: Q00855 |
| Total number of polymer chains | 1 |
| Total formula weight | 14064.19 |
| Authors | Ichikawa, S.,Takai, T.,Inoue, T.,Yuuki, T.,Okumura, Y.,Ogura, K.,Inagaki, F.,Hatanaka, H. (deposition date: 2004-10-15, release date: 2005-04-19, Last modification date: 2024-10-23) |
| Primary citation | Ichikawa, S.,Takai, T.,Inoue, T.,Yuuki, T.,Okumura, Y.,Ogura, K.,Inagaki, F.,Hatanaka, H. NMR Study on the Major Mite Allergen Der f 2: Its Refined Tertiary Structure, Epitopes for Monoclonal Antibodies and Characteristics Shared by ML Protein Group Members J.Biochem.(Tokyo), 137:255-263, 2005 Cited by PubMed Abstract: Group 2 major mite allergens Der f 2 and Der p 2 are classified into the recently identified group of MD-2-related lipid-recognition (ML) proteins, but the ligands and biological functions of these allergens are unknown. We have obtained a high-quality NMR structure for Der f 2, and found that it is more similar to the crystal structure of NPC2, a distant homologue, than to that of Der p 2, in terms of the separation and angle between the two major beta-sheets. This made us propose that ML proteins undergo clamshell-like motions that change the sizes of ligand-binding spaces inside their immunoglobulin-fold beta-sandwich to accommodate lipid molecules. This type of motion in lipopolysaccaride recognition of MD-2 is suggested to be likely as well by structural models. We also report the applicability of NMR differential exchange broadening experiments for complexes of intact monoclonal antibodies and antigens; using this technique, we have detected the conformational epitopes for monoclonal antibodies 15E11 and 13A4 as two separate surface patches. PubMed: 15809326DOI: 10.1093/jb/mvi039 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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