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1k9u

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(New page: 200px<br /><applet load="1k9u" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k9u, resolution 1.75&Aring;" /> '''Crystal Structure of...)
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[[Image:1k9u.jpg|left|200px]]<br /><applet load="1k9u" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1k9u, resolution 1.75&Aring;" />
caption="1k9u, resolution 1.75&Aring;" />
'''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==
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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.
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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==
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1K9U OCA].
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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]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:59:08 2007''
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''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


1k9u, resolution 1.75Å

Drag the structure with the mouse to rotate

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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