1a9v
From Proteopedia
(New page: 200px<br /><applet load="1a9v" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a9v" /> '''TERTIARY STRUCTURE OF THE MAJOR HOUSE DUST M...) |
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| - | [[Image:1a9v.gif|left|200px]]<br /><applet load="1a9v" size=" | + | [[Image:1a9v.gif|left|200px]]<br /><applet load="1a9v" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1a9v" /> | caption="1a9v" /> | ||
'''TERTIARY STRUCTURE OF THE MAJOR HOUSE DUST MITE ALLERGEN DER P 2, NMR, 10 STRUCTURES'''<br /> | '''TERTIARY STRUCTURE OF THE MAJOR HOUSE DUST MITE ALLERGEN DER P 2, NMR, 10 STRUCTURES'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Sensitization to indoor allergens, especially those of the house dust | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1A9V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Dermatophagoides_pteronyssinus Dermatophagoides pteronyssinus]. Full crystallographic information is available from [http:// | + | 1A9V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Dermatophagoides_pteronyssinus Dermatophagoides pteronyssinus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A9V OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Dermatophagoides pteronyssinus]] | [[Category: Dermatophagoides pteronyssinus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Benjamin, D | + | [[Category: Benjamin, D C.]] |
| - | [[Category: Mueller, G | + | [[Category: Mueller, G A.]] |
| - | [[Category: Rule, G | + | [[Category: Rule, G S.]] |
[[Category: allergen]] | [[Category: allergen]] | ||
[[Category: immunoglobulin fold]] | [[Category: immunoglobulin fold]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:42:27 2008'' |
Revision as of 09:42, 21 February 2008
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TERTIARY STRUCTURE OF THE MAJOR HOUSE DUST MITE ALLERGEN DER P 2, NMR, 10 STRUCTURES
Overview
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.
About this Structure
1A9V is a Single protein structure of sequence from Dermatophagoides pteronyssinus. Full crystallographic information is available from OCA.
Reference
Tertiary structure of the major house dust mite allergen Der p 2: sequential and structural homologies., Mueller GA, Benjamin DC, Rule GS, Biochemistry. 1998 Sep 15;37(37):12707-14. PMID:9737847
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