Fig. 5
Spatial structure and backbone dynamics of the major structural form of Ps-LTP1 in solution. a. The sets of the best 20 structures are superimposed over the backbone atoms in regions with well-defined structure (Cys4-Cys76). The disulfide bonds are shown in orange. The helices H1-H5 are color coded. b. Ribbon representation of the Ps-LTP1 spatial structure. The ribbon is colored according to obtained dynamical NMR data (see the legend in Fig. 3). The positively charged (Arg, Lys, N-terminal amide), negatively charged (Asp, C-terminal carboxylic group), and aromatic (Phe/Tyr) side chains/moieties are in blue, red, and green, respectively. The Pro residues are shown by cyan plates. The hydrogen bonds between side chain Asn68 (magenta) and CO groups of Tyr17 and Pro21 (red cylinders), and ionic bridge (Arg47 – C-terminus) are shown by broken lines. c. Two-sided view of the Ps-LTP1 spatial structure. The side chains of hydrophobic residues (Ala/Ile/Leu/Val) which form the internal cavity are colored in yellow. The residues that form the entrance into the internal hydrophobic cavity are marked by underlined lettering. The helices H1-H5 are color coded. d, e. Two-sided views of the surfaces of Ps-LTP1 and Pru p 3 (PDB ID 2ALG, [28]) molecules, superimposed over Cα atoms of the eight conserved Cys residues. The color code is similar to one used at the other panels, except that Pro residues are colored in yellow. The two IgE epitopes (one conformational Asn35-Ala46/Ser76-Tyr79 and one sequential Ala11-Pro25) are shown on the surface of Pru p 3 by thick black lines. The Ps-LTP1 region homologues to conformational epitope of Pru p 3 is shown by dotted line. The corresponding residues on the both molecules are shown by italic and underlined lettering. Ps-LTP1 molecules shown on the panels b, right c, and left d have identical orientation. The expected entrance into internal hydrophobic cavity is shown by arrow