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PDBsum entry 1a9v
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References listed in PDB file
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Key reference
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Title
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Tertiary structure of the major house dust mite allergen der p 2: sequential and structural homologies.
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Authors
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G.A.Mueller,
D.C.Benjamin,
G.S.Rule.
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Ref.
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Biochemistry, 1998,
37,
12707-12714.
[DOI no: ]
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PubMed id
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Abstract
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Sensitization to indoor allergens, especially those of the house dust mite, is
strongly correlated with the development of asthma. We report the tertiary
structure of the major house dust mite allergen, Der p 2, determined by NMR
methods. The structure of Der p 2 is a beta-barrel and is composed of two
three-stranded antiparallel beta-pleated sheets. This arrangement of
beta-strands is similar to the immunoglobulin fold with respect to the
orientation of the two sheets and the interactions of the strands. However, the
three-dimensional structure of Der p 2 aligns equivalently with a number of
proteins from different families within the immunoglobulin superfamily. The
structural homology with the highest significance score from analysis by DALI is
to Der f 2. Although Der p 2 and Der f 2 are 87% identical in amino acid
sequence, they align in three dimensions rather poorly (4.85 A RMSD; Z-score,
8.58). This unexpected finding is likely due to the different solution
conditions used during structure determination by NMR for both proteins. While
the structural comparisons did not elucidate a clear homologue for the function
of Der p 2 in mites, we report that Der p 2 is sequentially homologous to esr16.
This is a protein from moths that is expressed coincident with molting. Thus,
this homology has important ramifications for the study of mite allergy. The
structure of Der p 2 provides a useful tool in the design of recombinant
immunotherapeutics for the group 2 allergens.
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Secondary reference #1
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Title
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Expression and secondary structure determination by nmr methods of the major house dust mite allergen der p 2.
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Authors
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G.A.Mueller,
A.M.Smith,
D.C.Williams,
G.A.Hakkaart,
R.C.Aalberse,
M.D.Chapman,
G.S.Rule,
D.C.Benjamin.
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Ref.
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J Biol Chem, 1997,
272,
26893-26898.
[DOI no: ]
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PubMed id
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Figure 4.
Fig. 4. Two three-stranded  -sheets. The
predicted sheets are shown with the assigned long range HN-HN,
HN-H  , and H
-H NOESYs
indicated with dashed lines. The ovals encircle strongly
protected^ amides and their potential hydrogen bonding partner.
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Figure 5.
Fig. 5. Potential tertiary homologues. The global fold of Der
p 2 as determined by the alignment of the strands indicated in
Fig. 4 is shown. The global fold of a member of the
immunoglobulin superfamily (Ig) and alpha amylase inhibitor (AA)
are shown for comparison.
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The above figures are
reproduced from the cited reference
with permission from the ASBMB
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