Figure 3
Crystal structures for bovine p85α (105–319) wild type and containing patient-derived mutations. (a) Overlay of the bovine p85α (105–319) crystal (green and cyan, resolution 2.25 Å) with the crystal structure for the human p85α (105–319) protein fragment (1PBW; magenta and pink, resolution 2.0 Å). A homodimer of the bovine p85α BH domains was visible containing residues 113–297 for both components of the dimer. (b,c) p85α BH domain residues involved in the hydrophobic dimerization interface within the crystal lattice of the bovine protein (b; L161, M176, F177 and V181) and the human protein (c; L161, M176, I177 and V181). (d–g) Overlays of the crystal structures for p85α (105–319); wild type (green) and cancer-associated point mutants (yellow): E137K mutant (d), E217K mutant (e), R262T mutant (f), E297K mutant (g). Wild type and mutant sidechains are shown in stick representation. Lack of density for the K297 sidechain prevented inclusion of the sidechain, and it is modeled as Ala in the structure (e).
