Figure 5
Structures and locations of key residues within the SH3 and BH domains of p85α. (a) The human p85α SH3 domain with endometrial cancer-associated mutations shown (black) in relation to D21 (red) important for binding to proline-rich peptides containing a key arginine residue (blue)53. (b) The bovine p85α BH domain showing the residues that are important for Rab5 binding (red) and Rab5-GAP activity (red, orange). Endometrial cancer patient-derived mutations (black) and bladder cancer-associated mutations (brown) are also shown, including an in-frame deletion (Δ237–242), which was too unstable to purify. I177 (black) is both involved in BH–BH domain dimerization within the crystal structure and is a residue mutated in endometrial cancer.
