Diagrams of structural models for GIPC3.

<p>The ribbon diagrams for the 3D models of the PDZ domain in GIPC3. The wild type (A) and the mutated p.H170N (B) forms are shown. The key for structural features follow; the α-helices (red); the β-strands (blue); the β-turns (green); the loops (light gray); the side-chain for H170 in the wild type (pink) and the side-chain for N170 highlights the mutation (yellow). The surface diagrams show the surface topology and the interpolated charge distribution of the PDZ domain of GIPC3. Both the wild type (C) and the mutated p.H170N protein (D) are provided. The p.H170N mutated form shows one of the substrate molecular recognition pockets as being deeper with a larger volume compared to the wild type. The p.H170N mutated form shows the interpolated charge distribution as being reduced compared with the wild type. Structural and local environment for position 170 with the H-bond patterns are shown. The GIPC3 wild type (E) shows an absence of side-chain to main-chain H-bonds with the H170 side-chain; whilst the asparagine side-chain (yellow) in the mutated protein (F) forms side-chain to main-chain H-bonds.