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- Title
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.
- Authors
Ichikawa, Saori; Takai, Toshiro; Inoue, Takashi; Yuuki, Toshifumi; Okumura, Yasushi; Ogura, Kenji; Inagaki, Fuyuhiko; Hatanaka, Hideki
- 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.
- Publication
Journal of biochemistry, 2005, Vol 137, Issue 3, p255
- ISSN
0021-924X
- Publication type
Journal Article
- DOI
10.1093/jb/mvi039