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[[Image:1puo.gif|left|200px]]
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{{STRUCTURE_1puo|  PDB=1puo  |  SCENE=  }}
'''Crystal structure of Fel d 1- the major cat allergen'''


==Crystal structure of Fel d 1- the major cat allergen==
<StructureSection load='1puo' size='340' side='right'caption='[[1puo]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1puo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Felis_catus Felis catus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PUO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PUO FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1puo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1puo OCA], [https://pdbe.org/1puo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1puo RCSB], [https://www.ebi.ac.uk/pdbsum/1puo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1puo ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FEL1B_FELCA FEL1B_FELCA] [https://www.uniprot.org/uniprot/FEL1A_FELCA FEL1A_FELCA]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==Overview==
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<ref>PMID:12851385</ref>
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==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1PUO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Felis_catus Felis catus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PUO OCA].
</div>
<div class="pdbe-citations 1puo" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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:[http://www.ncbi.nlm.nih.gov/pubmed/12851385 12851385]
*[[Fel d 1|Fel d 1]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Felis catus]]
[[Category: Felis catus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Achour, A.]]
[[Category: Achour A]]
[[Category: Gronlund, H.]]
[[Category: Gronlund H]]
[[Category: Hage-Hamsten, M van.]]
[[Category: Kaiser L]]
[[Category: Kaiser, L.]]
[[Category: Ljunggren HG]]
[[Category: Ljunggren, H G.]]
[[Category: Sandalova T]]
[[Category: Sandalova, T.]]
[[Category: Schneider G]]
[[Category: Schneider, G.]]
[[Category: Van Hage-Hamsten M]]
[[Category: Cat allergen]]
[[Category: Secretoglobin]]
[[Category: Uteroglobin]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 05:30:18 2008''

Latest revision as of 10:13, 30 October 2024

Crystal structure of Fel d 1- the major cat allergenCrystal structure of Fel d 1- the major cat allergen

Structural highlights

1puo is a 2 chain structure with sequence from Felis catus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.85Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FEL1B_FELCA FEL1A_FELCA

Publication Abstract from PubMed

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.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Kaiser L, Gronlund H, Sandalova T, Ljunggren HG, van Hage-Hamsten M, Achour A, Schneider G. The crystal structure of the major cat allergen Fel d 1, a member of the secretoglobin family. J Biol Chem. 2003 Sep 26;278(39):37730-5. Epub 2003 Jul 8. PMID:12851385 doi:10.1074/jbc.M304740200

1puo, resolution 1.85Å

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