Figure 6 | Scientific Reports

Figure 6

From: Patient-derived mutations within the N-terminal domains of p85α impact PTEN or Rab5 binding and regulation

Figure 6

Modeled interface region between the human p85α BH domain and Rab5. (a) Overlay of the crystal structure of human Cdc42GAP (tan) – Cdc42 (blue) complex (PDB ID: 2NGR) with the human p85α BH domain (green; PDB ID: 1PBW) and the human Rab5-GTP analogue (15–184; grey; PDB ID: 1R2Q). The magnesium (teal) and GTP analogue (magenta) bound to Rab5 are indicated. Catalytically important arginine residues within Cdc42GAP (yellow) and p85α BH domain (orange) are shown. (b) Modeled human p85α BH domain (green) – Rab5 (grey) complex. The magnesium (teal) and GTP analogue (magenta) bound to Rab5 are indicated. Key p85α BH domain residues are shown: R151 (orange, important for GAP activity), and residues in red are important for Rab5 binding (L191, V263, R274). The location of patient-derived p85α BH mutations with significant impacts on Rab5 binding are shown in black (E137, I177, E217, E297).

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