FIGURE 4.

The negatively charged connecting loop of the DCAF1-FBD β-hairpin contributes to the binding to Merlin-FERM. A, the model of the connecting loop interacting with the highly positively charged F1/F3 cleft on Merlin-FERM. The figure was drawn using an electrostatic surface charge potential map with blue for the positive charge potential and red for the negative charge potential. The positively charged residues involved in forming the cleft are labeled. B, the structure of the FERM domain of Radixin in complex with the headgroup of phosphatidylinositol 4,5-bisphosphate (Protein Data Bank code 1GC6) was shown in the same presentation mode as A for comparison. The headgroup structure is highlighted by a yellow circle.