NMR Studies of the C-Terminus of alpha4 Reveal Possible Mechanism of Its Interaction with MID1 and Protein Phosphatase 2A
Figure 6
Proposed surfaces of interaction.
A. Surface depiction of the two binding interfaces of alpha45 that could interact with the Bbox1 domain and PP2A simultaneously. B. Ribbon representation of the A- (scaffolding (PR65), colored gray) and C- (catalytic, colored yellow) subunits of PP2A, pdb accession code 3DW8. PR65 adopts a helix-turn-helix HEAT repeat structure. All glutamic and aspartic acids are shown in red on the A(PR65)-subunit. Located near the N-terminus of PR65 is a large negative patch, depicted by surface representation (colored red) that could accommodate the positively charged surface of alpha45. This is also the same surface on which the B- (regulatory, B55) subunit of PP2A binds. The alpha4 N-terminal binding site on PP2Ac is shown in orange.