1PUO

Crystal structure of Fel d 1- the major cat allergen

Summary for 1PUO

• Entry DOI: 10.2210/pdb1puo/pdb
• Descriptor: Major allergen I polypeptide, fused chain 2, chain 1, (4S)-2-METHYL-2,4-PENTANEDIOL (3 entities in total)
• Functional Keywords: cat allergen, uteroglobin, secretoglobin, allergen
• Biological source: Felis catus (domestic cat); More
• Total number of polymer chains: 2
• Total formula weight: 38622.44

Authors

Kaiser, L.,Gronlund, H.,Sandalova, T.,Ljunggren, H.G.,van Hage-Hamsten, M.,Achour, A.,Schneider, G. (deposition date: 2003-06-25, release date: 2003-10-14, Last modification date: 2024-10-30)

Primary citation

Kaiser, L.,Gronlund, H.,Sandalova, T.,Ljunggren, H.G.,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., 278:37730-37735, 2003

PubMed Abstract: 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.

PubMed: 12851385
DOI: 10.1074/jbc.M304740200

Experimental method

X-RAY DIFFRACTION (1.85 Å)