2JMH
NMR solution structure of Blo t 5, a major mite allergen from Blomia tropicalis
Summary for 2JMH
| Entry DOI | 10.2210/pdb2jmh/pdb |
| Descriptor | Mite allergen Blo t 5 (1 entity in total) |
| Functional Keywords | allergen, dust mites, blomia tropicalis, blo t 5, group 5 |
| Biological source | Blomia tropicalis |
| Total number of polymer chains | 1 |
| Total formula weight | 14058.82 |
| Authors | Naik, M.T.,Chang, C.,Kuo, I.,Chua, K.,Huang, T. (deposition date: 2006-11-12, release date: 2007-11-13, Last modification date: 2023-12-20) |
| Primary citation | Naik, M.T.,Chang, C.F.,Kuo, I.C.,Kung, C.C.,Yi, F.C.,Chua, K.Y.,Huang, T.H. Roles of Structure and Structural Dynamics in the Antibody Recognition of the Allergen Proteins: An NMR Study on Blomia tropicalis Major Allergen Structure, 16:125-136, 2008 Cited by PubMed Abstract: Blo t 5 is the major allergen from Blomia tropicalis mites and shows strong IgE reactivity with up to 90% of asthmatic and rhinitis patients' sera. The NMR solution structure of Blo t 5 comprises three long alpha helices, forming a coiled-coil, triple-helical bundle with a left-handed twist. TROSY-NMR experiments were used to study Blo t 5 interaction with the Fab' of a specific monoclonal antibody, mAb 4A7. The mAb epitope comprises two closely spaced surfaces, I and II, connected by a sharp turn and bearing critical residues Asn46 and Lys47 on one surface, and Lys54 and Arg57 on the other. This discontinuous epitope overlaps with the human IgE epitope(s) of Blo t 5. Epitope surface II is further predicted to undergo conformational exchange in the millisecond to microsecond range. The results presented are critical for the design of a hypoallergenic Blo t 5 for efficacious immunotherapy of allergic diseases. PubMed: 18184590DOI: 10.1016/j.str.2007.10.022 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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