Fig. 1

Randomly PEGylated soluble HLA-G2 homodimer protein in lysine residues. (A) SPR analysis of HLA-G2 (6.2 μM, left) or PEGylated HLA-G2 in lysine residues (randomPEG-HLA-G2, 5.3 μM, right) to the immobilized PIR-B. Each soluble HLA-G2 homodimer protein was injected over the immobilized PIR-B (3000 RU, black line) and negative control BSA (2000 RU, gray line). The response of the SPR results to BSA was due to buffer mismatch and nonspecific interactions between the analytes and BSA. (B) Schematic diagram of the domain structure (left) and the model structure (right) of the soluble HLA-G2 homodimer³. The original Cys42 (green circle) and lysine residues (blue circle) are shown in the schematic structures (left). Three lysine residues are shown in the blue stick model (right). K183, which is not visible in the crystal structure of the soluble HLA-G1 monomer (PDB ID: 2DYP), is shown in the blue circle (right).