1z3q
From Proteopedia
(New page: 200px<br /><applet load="1z3q" size="450" color="white" frame="true" align="right" spinBox="true" caption="1z3q, resolution 1.70Å" /> '''Resolution of the st...) |
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| - | [[Image:1z3q.gif|left|200px]]<br /><applet load="1z3q" size=" | + | [[Image:1z3q.gif|left|200px]]<br /><applet load="1z3q" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1z3q, resolution 1.70Å" /> | caption="1z3q, resolution 1.70Å" /> | ||
'''Resolution of the structure of the allergenic and antifungal banana fruit thaumatin-like protein at 1.7A'''<br /> | '''Resolution of the structure of the allergenic and antifungal banana fruit thaumatin-like protein at 1.7A'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of a thaumatin-like protein from banana (Musa acuminata) | + | The structure of a thaumatin-like protein from banana (Musa acuminata) fruit, an allergen with antifungal properties, was solved at 1.7-A-resolution, by X-ray crystallography. Though the banana protein exhibits a very similar overall fold as thaumatin it markedly differs from the sweet-tasting protein by the presence of a surface exposed electronegative cleft. Due to the presence of this electronegative cleft, the banana thaumatin-like protein (Ban-TLP) acquires a strong (local) electronegative character that eventually explains the observed antifungal activity. Our structural analysis also revealed the presence of conserved residues of exposed epitopic determinants that are presumably responsible for the allergenic properties of banana fruit towards susceptible individuals, and provided evidence that the Ban-TLP shares some structurally highly conserved IgE-binding epitopes with thaumatin-like proteins from fruits or pollen from other plants. In addition, some overlap was detected between the predicted IgE-binding epitopes of the Ban-TLP and IgE-binding epitopes previously identified in the mountain cedar Jun a 3 TLP aeroallergen. The presence of these common epitopes offers a molecular basis for the cross-reactivity between aeroallergens and fruit allergens. |
==About this Structure== | ==About this Structure== | ||
| - | 1Z3Q is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Musa_acuminata Musa acuminata] with EDO as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1Z3Q is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Musa_acuminata Musa acuminata] with <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z3Q OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Barre, A.]] | [[Category: Barre, A.]] | ||
| - | [[Category: Damme, E | + | [[Category: Damme, E J.M Van.]] |
[[Category: Leone, P.]] | [[Category: Leone, P.]] | ||
[[Category: Menu-Bouaouiche, L.]] | [[Category: Menu-Bouaouiche, L.]] | ||
[[Category: Payan, F.]] | [[Category: Payan, F.]] | ||
| - | [[Category: Peumans, W | + | [[Category: Peumans, W J.]] |
[[Category: Rouge, P.]] | [[Category: Rouge, P.]] | ||
[[Category: Roussel, A.]] | [[Category: Roussel, A.]] | ||
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[[Category: beta sandwich]] | [[Category: beta sandwich]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:11:51 2008'' |
Revision as of 14:11, 21 February 2008
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Resolution of the structure of the allergenic and antifungal banana fruit thaumatin-like protein at 1.7A
Overview
The structure of a thaumatin-like protein from banana (Musa acuminata) fruit, an allergen with antifungal properties, was solved at 1.7-A-resolution, by X-ray crystallography. Though the banana protein exhibits a very similar overall fold as thaumatin it markedly differs from the sweet-tasting protein by the presence of a surface exposed electronegative cleft. Due to the presence of this electronegative cleft, the banana thaumatin-like protein (Ban-TLP) acquires a strong (local) electronegative character that eventually explains the observed antifungal activity. Our structural analysis also revealed the presence of conserved residues of exposed epitopic determinants that are presumably responsible for the allergenic properties of banana fruit towards susceptible individuals, and provided evidence that the Ban-TLP shares some structurally highly conserved IgE-binding epitopes with thaumatin-like proteins from fruits or pollen from other plants. In addition, some overlap was detected between the predicted IgE-binding epitopes of the Ban-TLP and IgE-binding epitopes previously identified in the mountain cedar Jun a 3 TLP aeroallergen. The presence of these common epitopes offers a molecular basis for the cross-reactivity between aeroallergens and fruit allergens.
About this Structure
1Z3Q is a Protein complex structure of sequences from Musa acuminata with as ligand. Full crystallographic information is available from OCA.
Reference
Resolution of the structure of the allergenic and antifungal banana fruit thaumatin-like protein at 1.7-A., Leone P, Menu-Bouaouiche L, Peumans WJ, Payan F, Barre A, Roussel A, Van Damme EJ, Rouge P, Biochimie. 2006 Jan;88(1):45-52. Epub 2005 Aug 8. PMID:16085352
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