FIGURE 8.

Mapping the 2′F B6min-hβ₂m binding site. A, the residues in hβ₂m that show the largest decrease in intensity upon interaction with 2′F B6min are shown in red on the structure of hβ₂m (gray schematic) and predominantly involve residues in the A, B, E, and D β-strands of hβ₂m. By contrast, the C, F, and G β-strands show relatively little change in intensity (bottom). B, surface representation of hβ₂m highlighting the interface residues (red). C, the 2′F B6min-hβ₂m binding interface involves seven aromatic residues (light green), seven positively charged residues (blue), and seven negatively charged residues (pink).