1puo

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1puo, resolution 1.85Å

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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 MPD 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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