1a9v: Difference between revisions

Revision as of 16:27, 30 June 2008

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File:1a9v.png

Template:STRUCTURE 1a9v

TERTIARY STRUCTURE OF THE MAJOR HOUSE DUST MITE ALLERGEN DER P 2, NMR, 10 STRUCTURESTERTIARY STRUCTURE OF THE MAJOR HOUSE DUST MITE ALLERGEN DER P 2, NMR, 10 STRUCTURES

Template:ABSTRACT PUBMED 9737847

About this StructureAbout this Structure

1A9V is a Single protein structure of sequence from Dermatophagoides pteronyssinus. Full experimental information is available from OCA.

ReferenceReference

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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-'''TERTIARY STRUCTURE OF THE MAJOR HOUSE DUST MITE ALLERGEN DER P 2, NMR, 10 STRUCTURES'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_9737847}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9737847 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_9737847}}
 ==About this Structure==
-A9V is a [[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].
+A9V is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Dermatophagoides_pteronyssinus Dermatophagoides pteronyssinus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A9V OCA].
 ==Reference==
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 [[Category: Allergen]]
 [[Category: Immunoglobulin fold]]
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