1k9u
From Proteopedia
(New page: 200px<br /><applet load="1k9u" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k9u, resolution 1.75Å" /> '''Crystal Structure of...) |
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- | [[Image:1k9u.jpg|left|200px]]<br /><applet load="1k9u" size=" | + | [[Image:1k9u.jpg|left|200px]]<br /><applet load="1k9u" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1k9u, resolution 1.75Å" /> | caption="1k9u, resolution 1.75Å" /> | ||
'''Crystal Structure of the Calcium-Binding Pollen Allergen Phl p 7 (Polcalcin) at 1.75 Angstroem'''<br /> | '''Crystal Structure of the Calcium-Binding Pollen Allergen Phl p 7 (Polcalcin) at 1.75 Angstroem'''<br /> | ||
==Overview== | ==Overview== | ||
- | The timothy grass pollen allergen Phl p 7 assembles most of the IgE | + | The timothy grass pollen allergen Phl p 7 assembles most of the IgE epitopes of a novel family of 2 EF-hand calcium-binding proteins and therefore represents a diagnostic marker allergen and vaccine candidate for immunotherapy. Here we report the first three-dimensional structure of a representative of the 2 EF-hand allergen family, Phl p 7, in the calcium-bound form. The protein occurs as a novel dimer assembly with unique features: in contrast to well known EF-hand proteins such as calmodulin, parvalbumin or the S100 proteins, Phl p 7 adopts an extended conformation. Two protein monomers assemble in a head-to-tail arrangement with domain-swapped EF-hand pairing. The intertwined dimer adopts a barrel-like structure with an extended hydrophobic cavity providing a ligand-binding site. Calcium binding acts as a conformational switch between an open and a closed dimeric form of Phl p 7. These findings are interesting in the context of lipid- and calcium-dependent pollen tube growth. Furthermore, the structure of Phl p 7 allows for the rational development of vaccine strategies for treatment of sensitized allergic patients. |
==About this Structure== | ==About this Structure== | ||
- | 1K9U is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Phleum_pratense Phleum pratense] with SO4 and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1K9U is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Phleum_pratense Phleum pratense] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K9U OCA]. |
==Reference== | ==Reference== | ||
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[[Category: pollen allergen]] | [[Category: pollen allergen]] | ||
- | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:31:43 2008'' |
Revision as of 11:31, 21 February 2008
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Crystal Structure of the Calcium-Binding Pollen Allergen Phl p 7 (Polcalcin) at 1.75 Angstroem
Overview
The timothy grass pollen allergen Phl p 7 assembles most of the IgE epitopes of a novel family of 2 EF-hand calcium-binding proteins and therefore represents a diagnostic marker allergen and vaccine candidate for immunotherapy. Here we report the first three-dimensional structure of a representative of the 2 EF-hand allergen family, Phl p 7, in the calcium-bound form. The protein occurs as a novel dimer assembly with unique features: in contrast to well known EF-hand proteins such as calmodulin, parvalbumin or the S100 proteins, Phl p 7 adopts an extended conformation. Two protein monomers assemble in a head-to-tail arrangement with domain-swapped EF-hand pairing. The intertwined dimer adopts a barrel-like structure with an extended hydrophobic cavity providing a ligand-binding site. Calcium binding acts as a conformational switch between an open and a closed dimeric form of Phl p 7. These findings are interesting in the context of lipid- and calcium-dependent pollen tube growth. Furthermore, the structure of Phl p 7 allows for the rational development of vaccine strategies for treatment of sensitized allergic patients.
About this Structure
1K9U is a Single protein structure of sequence from Phleum pratense with and as ligands. Full crystallographic information is available from OCA.
Reference
The cross-reactive calcium-binding pollen allergen, Phl p 7, reveals a novel dimer assembly., Verdino P, Westritschnig K, Valenta R, Keller W, EMBO J. 2002 Oct 1;21(19):5007-16. PMID:12356717
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