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1WRF

Refined solution structure of Der f 2, The Major Mite Allergen from Dermatophagoides farinae

Summary for 1WRF
Entry DOI10.2210/pdb1wrf/pdb
Related1AHK 1AHM
DescriptorMite group 2 allergen Der f 2 (1 entity in total)
Functional Keywordsallergen, immunoglobulin fold
Biological sourceDermatophagoides farinae (American house dust mite)
Cellular locationSecreted: Q00855
Total number of polymer chains1
Total formula weight14064.19
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 citationIchikawa, 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: 15809326
DOI: 10.1093/jb/mvi039
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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