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PDBsum entry 1ahk
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References listed in PDB file
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Key reference
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Title
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Solution structure of der f 2, The major mite allergen for atopic diseases.
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Authors
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S.Ichikawa,
H.Hatanaka,
T.Yuuki,
N.Iwamoto,
S.Kojima,
C.Nishiyama,
K.Ogura,
Y.Okumura,
F.Inagaki.
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Ref.
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J Biol Chem, 1998,
273,
356-360.
[DOI no: ]
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PubMed id
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Abstract
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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.
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Figure 2.
Fig. 2. Tertiary structure of Der f 2. a, Best fit
superpositions of the backbone atoms (N, C^  , C
 ) of the 10
final structures of Der f 2. Amino acid residue^ numbers are
shown every ten residues. b, Ribbon diagrams of the^ mean
structure of Der f 2. The start and end residue numbers of^ the
 -strands are
also shown. Both figures were produced by the^ program MOLSCRIPT
(44) and shown in stereo. Color changes from red (N terminus) to
blue (C terminus).
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Figure 5.
Fig. 5. Partial characterization of IgE epitope areas.
The molecular surface of Der f 2 was produced by the program
GRASP (45) and colored according to the results from the
site-directed mutagenesis experiments (42). Red, residues whose
substitution decreased^ IgE binding; blue, residues whose
substitution did not decrease^ IgE binding; white, residues that
were not tested. The top figure^ can be related to Fig. 2 by
105° x rotation, and the bottom can be related to the top by
180° x rotation.
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The above figures are
reprinted
by permission from the ASBMB:
J Biol Chem
(1998,
273,
356-360)
copyright 1998.
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