1puo
From Proteopedia
(New page: 200px<br /><applet load="1puo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1puo, resolution 1.85Å" /> '''Crystal structure of...) |
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| - | [[Image:1puo.gif|left|200px]]<br /><applet load="1puo" size=" | + | [[Image:1puo.gif|left|200px]]<br /><applet load="1puo" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1puo, resolution 1.85Å" /> | caption="1puo, resolution 1.85Å" /> | ||
'''Crystal structure of Fel d 1- the major cat allergen'''<br /> | '''Crystal structure of Fel d 1- the major cat allergen'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The domestic cat (Felis domesticus) is one of the most important causes of | + | The domestic cat (Felis domesticus) is one of the most important causes of allergic asthma worldwide. The dominating cat allergen, Fel d 1, is composed of two heterodimers. Recently, it has been shown that recombinant Fel d 1, consisting of chain 2 and chain 1 fused together without additional linker, has immunological properties indistinguishable from the natural heterodimeric protein. Herein, we report the crystal structure of recombinant monomeric Fel d 1 at 1.85-A resolution, determined by multi-wavelength anomalous diffraction using selenomethionine substituted protein. Fel d 1 is an all-helical protein and consists of eight helices. The two halves of the recombinant Fel d 1 molecule, corresponding to the wild-type Fel d 1 chains, are very similar in three-dimensional structure, despite the lack of significant sequence identity. The structure of the Fel d 1 presents a striking similarity to that of uteroglobin, a steroid-inducible cytokine-like molecule with anti-inflammatory and immunomodulatory properties. An internal, asymmetric cavity is formed in the Fel d 1 that could bind an endogenous ligand. The distribution of residues lining this cavity suggests that such a ligand must be amphipathic. The structure of Fel d 1 displays the localization of three previously defined Fel d 1 IgE epitopes on the surface of the protein. The three-dimensional structure provides a framework for rational design of hypoallergenic mutants aimed for treatment of cat allergy. |
==About this Structure== | ==About this Structure== | ||
| - | 1PUO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Felis_catus Felis catus] with MPD as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1PUO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Felis_catus Felis catus] with <scene name='pdbligand=MPD:'>MPD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PUO OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Achour, A.]] | [[Category: Achour, A.]] | ||
[[Category: Gronlund, H.]] | [[Category: Gronlund, H.]] | ||
| - | [[Category: Hage-Hamsten, M | + | [[Category: Hage-Hamsten, M van.]] |
[[Category: Kaiser, L.]] | [[Category: Kaiser, L.]] | ||
| - | [[Category: Ljunggren, H | + | [[Category: Ljunggren, H G.]] |
[[Category: Sandalova, T.]] | [[Category: Sandalova, T.]] | ||
[[Category: Schneider, G.]] | [[Category: Schneider, G.]] | ||
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[[Category: uteroglobin]] | [[Category: uteroglobin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:32:42 2008'' |
Revision as of 12:32, 21 February 2008
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Crystal structure of Fel d 1- the major cat allergen
Overview
The domestic cat (Felis domesticus) is one of the most important causes of allergic asthma worldwide. The dominating cat allergen, Fel d 1, is composed of two heterodimers. Recently, it has been shown that recombinant Fel d 1, consisting of chain 2 and chain 1 fused together without additional linker, has immunological properties indistinguishable from the natural heterodimeric protein. Herein, we report the crystal structure of recombinant monomeric Fel d 1 at 1.85-A resolution, determined by multi-wavelength anomalous diffraction using selenomethionine substituted protein. Fel d 1 is an all-helical protein and consists of eight helices. The two halves of the recombinant Fel d 1 molecule, corresponding to the wild-type Fel d 1 chains, are very similar in three-dimensional structure, despite the lack of significant sequence identity. The structure of the Fel d 1 presents a striking similarity to that of uteroglobin, a steroid-inducible cytokine-like molecule with anti-inflammatory and immunomodulatory properties. An internal, asymmetric cavity is formed in the Fel d 1 that could bind an endogenous ligand. The distribution of residues lining this cavity suggests that such a ligand must be amphipathic. The structure of Fel d 1 displays the localization of three previously defined Fel d 1 IgE epitopes on the surface of the protein. The three-dimensional structure provides a framework for rational design of hypoallergenic mutants aimed for treatment of cat allergy.
About this Structure
1PUO is a Single protein structure of sequence from Felis catus with as ligand. Full crystallographic information is available from OCA.
Reference
The crystal structure of the major cat allergen Fel d 1, a member of the secretoglobin family., Kaiser L, Gronlund H, Sandalova T, Ljunggren HG, van Hage-Hamsten M, Achour A, Schneider G, J Biol Chem. 2003 Sep 26;278(39):37730-5. Epub 2003 Jul 8. PMID:12851385
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