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New page: left|200px<br /><applet load="1xwv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xwv, resolution 1.83Å" /> '''Structure of the hou...
 
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[[Image:1xwv.gif|left|200px]]<br /><applet load="1xwv" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1xwv.gif|left|200px]]<br /><applet load="1xwv" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1xwv, resolution 1.83&Aring;" />
caption="1xwv, resolution 1.83&Aring;" />
'''Structure of the house dust mite allergen Der f 2: Implications for function and molecular basis of IgE cross-reactivity'''<br />
'''Structure of the house dust mite allergen Der f 2: Implications for function and molecular basis of IgE cross-reactivity'''<br />


==Overview==
==Overview==
The X-ray structure of the group 2 major allergen from Dermatophagoides, farinae (Der f 2) was determined to 1.83 A resolution. The overall Der f 2, structure comprises a single domain of immunoglobulin fold with two, anti-parallel beta-sheets. A large hydrophobic cavity is formed in the, interior of Der f 2. Structural comparisons to distantly related proteins, suggest a role in lipid binding. Immunoglobulin E (IgE) cross-reactivity, between group 2 house dust mite major allergens can be explained by, conserved surface areas representing IgE binding epitopes.
The X-ray structure of the group 2 major allergen from Dermatophagoides farinae (Der f 2) was determined to 1.83 A resolution. The overall Der f 2 structure comprises a single domain of immunoglobulin fold with two anti-parallel beta-sheets. A large hydrophobic cavity is formed in the interior of Der f 2. Structural comparisons to distantly related proteins suggest a role in lipid binding. Immunoglobulin E (IgE) cross-reactivity between group 2 house dust mite major allergens can be explained by conserved surface areas representing IgE binding epitopes.


==About this Structure==
==About this Structure==
1XWV 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 PE3 and XPE as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XWV OCA].  
1XWV 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=PE3:'>PE3</scene> and <scene name='pdbligand=XPE:'>XPE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XWV OCA].  


==Reference==
==Reference==
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[[Category: Bolwig, C.]]
[[Category: Bolwig, C.]]
[[Category: Gajhede, M.]]
[[Category: Gajhede, M.]]
[[Category: Johannessen, B.R.]]
[[Category: Johannessen, B R.]]
[[Category: Kastrup, J.S.]]
[[Category: Kastrup, J S.]]
[[Category: Kristensen, O.]]
[[Category: Kristensen, O.]]
[[Category: Larsen, J.N.]]
[[Category: Larsen, J N.]]
[[Category: Lund, K.]]
[[Category: Lund, K.]]
[[Category: Skov, L.K.]]
[[Category: Skov, L K.]]
[[Category: Spangfort, M.]]
[[Category: Spangfort, M.]]
[[Category: PE3]]
[[Category: PE3]]
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[[Category: beta sheets]]
[[Category: beta sheets]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 06:23:49 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:59:29 2008''

Revision as of 13:59, 21 February 2008

File:1xwv.gif


1xwv, resolution 1.83Å

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Structure of the house dust mite allergen Der f 2: Implications for function and molecular basis of IgE cross-reactivity

Overview

The X-ray structure of the group 2 major allergen from Dermatophagoides farinae (Der f 2) was determined to 1.83 A resolution. The overall Der f 2 structure comprises a single domain of immunoglobulin fold with two anti-parallel beta-sheets. A large hydrophobic cavity is formed in the interior of Der f 2. Structural comparisons to distantly related proteins suggest a role in lipid binding. Immunoglobulin E (IgE) cross-reactivity between group 2 house dust mite major allergens can be explained by conserved surface areas representing IgE binding epitopes.

About this Structure

1XWV is a Single protein structure of sequence from Dermatophagoides farinae with PE3 and XPE as ligands. Full crystallographic information is available from OCA.

Reference

Structure of the house dust mite allergen Der f 2: implications for function and molecular basis of IgE cross-reactivity., Johannessen BR, Skov LK, Kastrup JS, Kristensen O, Bolwig C, Larsen JN, Spangfort M, Lund K, Gajhede M, FEBS Lett. 2005 Feb 14;579(5):1208-12. Epub 2005 Jan 21. PMID:15710415

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