2f08

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(New page: 200px<br /><applet load="2f08" size="450" color="white" frame="true" align="right" spinBox="true" caption="2f08, resolution 2.20&Aring;" /> '''Crystal structure of...)
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caption="2f08, resolution 2.20&Aring;" />
caption="2f08, resolution 2.20&Aring;" />
'''Crystal structure of a major house dust mite allergen, Derf 2'''<br />
'''Crystal structure of a major house dust mite allergen, Derf 2'''<br />
==Overview==
==Overview==
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Pyroglyphid house dust mites are a major source of allergens in house, dust. Mite allergens sensitize and induce asthma, rhinitis, and eczema in, a large portion of patients with allergic diseases. Here, the crystal, structure of a major mite allergen, Derf 2, derived from Dermatophagoides, farinae was solved by single isomorphous replacement method with anomalous, scattering (SIRAS) at 2.1A resolution. The present study also demonstrated, that the conformation of the allergen was critical in the determination of, Th1/Th2 shift based on physicochemical and immunological analyses. This, indicates that rigidly folded and singly dispersed structure is, essentially required for the generation of Th2 type cells by the allergen, while conformational variant protein leads to Th1 skewing, irrespective of, the same amino acid sequence. This structure/function relationship may, allow us to develop a novel strategy for hyposensitization therapy in, patients with allergic diseases triggered by house dust mite allergens.
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Pyroglyphid house dust mites are a major source of allergens in house dust. Mite allergens sensitize and induce asthma, rhinitis, and eczema in a large portion of patients with allergic diseases. Here, the crystal structure of a major mite allergen, Derf 2, derived from Dermatophagoides farinae was solved by single isomorphous replacement method with anomalous scattering (SIRAS) at 2.1A resolution. The present study also demonstrated that the conformation of the allergen was critical in the determination of Th1/Th2 shift based on physicochemical and immunological analyses. This indicates that rigidly folded and singly dispersed structure is essentially required for the generation of Th2 type cells by the allergen, while conformational variant protein leads to Th1 skewing, irrespective of the same amino acid sequence. This structure/function relationship may allow us to develop a novel strategy for hyposensitization therapy in patients with allergic diseases triggered by house dust mite allergens.
==About this Structure==
==About this Structure==
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2F08 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Dermatophagoides_farinae Dermatophagoides farinae] with P4C as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2F08 OCA].
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2F08 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Dermatophagoides_farinae Dermatophagoides farinae] with <scene name='pdbligand=P4C:'>P4C</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F08 OCA].
==Reference==
==Reference==
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[[Category: immunoglobulin fold]]
[[Category: immunoglobulin fold]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 10:15:56 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:16:22 2008''

Revision as of 15:16, 21 February 2008


2f08, resolution 2.20Å

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Crystal structure of a major house dust mite allergen, Derf 2

Overview

Pyroglyphid house dust mites are a major source of allergens in house dust. Mite allergens sensitize and induce asthma, rhinitis, and eczema in a large portion of patients with allergic diseases. Here, the crystal structure of a major mite allergen, Derf 2, derived from Dermatophagoides farinae was solved by single isomorphous replacement method with anomalous scattering (SIRAS) at 2.1A resolution. The present study also demonstrated that the conformation of the allergen was critical in the determination of Th1/Th2 shift based on physicochemical and immunological analyses. This indicates that rigidly folded and singly dispersed structure is essentially required for the generation of Th2 type cells by the allergen, while conformational variant protein leads to Th1 skewing, irrespective of the same amino acid sequence. This structure/function relationship may allow us to develop a novel strategy for hyposensitization therapy in patients with allergic diseases triggered by house dust mite allergens.

About this Structure

2F08 is a Single protein structure of sequence from Dermatophagoides farinae with as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure and some properties of a major house dust mite allergen, Derf 2., Suzuki M, Tanaka Y, Korematsu S, Mikami B, Minato N, Biochem Biophys Res Commun. 2006 Jan 13;339(2):679-86. Epub 2005 Nov 21. PMID:16313885

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