Structural characteristics of lipocalin allergens: Crystal structure of the immunogenic dog allergen Can f 6
Fig 5
Comparison of predicted post translational modification sites.
(A) Summary of glycosylation sites. (B) Three N-linked glycosylation residues (blue spheres) are predicted at Asn35, 52, and 75 in Can f 6; one in Can f 2 at Asn27; and two in Equ c 1 at Asn37 and 68. All these sites are on loops. The O-linked glycosylation site predicted in Can f 6 (purple spheres) is at the end of the C-terminus (Ser166) and is not modeled because this region of the structure is disordered. (C) Predicted phosphorylation sites (orange spheres). Phosphorylated Tyr22 and Ser18 in human tear lipocalin are present and labeled in Can f 6.