3L4R

Crystal structure of the dog lipocalin allergen Can f 2 and implications for cross-reactivity to the cat allergen Fel d 4

Summary for 3L4R

• Entry DOI: 10.2210/pdb3l4r/pdb
• Descriptor: Minor allergen Can f 2, GLYCEROL (3 entities in total)
• Functional Keywords: lipocalin allergen, allergen, disulfide bond, secreted, transport, lipid binding protein
• Biological source: Canis familiaris (dogs)
• Cellular location: Secreted: O18874
• Total number of polymer chains: 1
• Total formula weight: 19565.74

Authors

Madhurantakam, C.,Nilsson, O.B.,Gronlund, H.,Achour, A. (deposition date: 2009-12-21, release date: 2010-05-26, Last modification date: 2024-11-20)

Primary citation

Madhurantakam, C.,Nilsson, O.B.,Uchtenhagen, H.,Konradsen, J.,Saarne, T.,Hogbom, E.,Sandalova, T.,Gronlund, H.,Achour, A.
Crystal Structure of the Dog Lipocalin Allergen Can f 2: Implications for Cross-reactivity to the Cat Allergen Fel d 4
J.Mol.Biol., 401:68-83, 2010

PubMed Abstract: The dog lipocalin allergen Can f 2 is an important cause of allergic sensitization in humans worldwide. Here, the first crystal structure of recombinant rCan f 2 at 1.45 A resolution displays a classical lipocalin fold with a conserved Gly-Xaa-Trp motif, in which Trp19 stabilizes the overall topology of the monomeric rCan f 2. Phe38 and Tyr84 localized on the L1 and L5 loops, respectively, control access to the highly hydrophobic calyx. Although the rCan f 2 calyx is nearly identical with the aero-allergens MUP1, Equ c 1 and A2U from mouse, horse and rat, respectively, no IgE cross-reactivity was found using sera from five mono-sensitized subjects. However, clear IgE cross-reactivity was demonstrated between Can f 2 and the cat allergen Fel d 4, although they share less than 22% sequence identity. This suggests a role for these allergens in co-sensitization between cat- and dog-allergic patients.

PubMed: 20621650
DOI: 10.1016/j.jmb.2010.05.043

Experimental method

X-RAY DIFFRACTION (1.45 Å)